HEADER TRANSFERASE 04-MAR-16 5FY7
TITLE CRYSTAL STRUCTURE OF JMJC DOMAIN OF HUMAN HISTONE DEMETHYLASE UTY IN
TITLE 2 COMPLEX WITH SUCCINATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: HISTONE DEMETHYLASE UTY;
COMPND 3 CHAIN: A, B;
COMPND 4 FRAGMENT: JMJC DOMAIN, RESIDUES 878-1347;
COMPND 5 SYNONYM: UBIQUITOUSLY-TRANSCRIBED TPR PROTEIN ON THE Y CHROMOSOME, U
COMPND 6 BIQUITOUSLY-TRANSCRIBED Y CHROMOSOME TETRATRICOPEPTIDE REPEAT
COMPND 7 PROTEIN;
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: SPODOPTERA FRUGIPERDA;
SOURCE 6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108;
SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: SF9
KEYWDS TRANSFERASE, TCA INTERMEDIATE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.NOWAK,T.KROJER,C.JOHANSSON,C.GILEADI,K.KUPINSKA,F.VON DELFT,
AUTHOR 2 C.H.ARROWSMITH,C.BOUNTRA,A.EDWARDS,U.OPPERMANN
REVDAT 4 10-JAN-24 5FY7 1 REMARK LINK
REVDAT 3 24-JAN-18 5FY7 1 JRNL
REVDAT 2 13-APR-16 5FY7 1 REMARK HET HETNAM FORMUL
REVDAT 2 2 1 LINK SITE HETATM MASTER
REVDAT 1 16-MAR-16 5FY7 0
JRNL AUTH R.NOWAK,T.KROJER,C.JOHANSSON,C.GILEADI,K.KUPINSKA,
JRNL AUTH 2 F.VON DELFT,C.H.ARROWSMITH,C.BOUNTRA,A.EDWARDS,U.OPPERMANN
JRNL TITL CRYSTAL STRUCTURE OF JMJC DOMAIN OF HUMAN HISTONE
JRNL TITL 2 DEMETHYLASE UTY IN COMPLEX WITH SUCCINATE
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 1.86 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) : 1.86
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 55.39
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 102876
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 : 0.225
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 5112
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 55.4095 - 5.7774 1.00 3509 168 0.1571 0.1843
REMARK 3 2 5.7774 - 4.5864 1.00 3331 201 0.1471 0.1644
REMARK 3 3 4.5864 - 4.0068 1.00 3333 164 0.1371 0.1968
REMARK 3 4 4.0068 - 3.6405 1.00 3332 169 0.1624 0.1843
REMARK 3 5 3.6405 - 3.3796 1.00 3311 153 0.1703 0.1966
REMARK 3 6 3.3796 - 3.1804 1.00 3283 156 0.1842 0.2279
REMARK 3 7 3.1804 - 3.0211 1.00 3261 186 0.1867 0.2240
REMARK 3 8 3.0211 - 2.8896 1.00 3275 165 0.1867 0.2205
REMARK 3 9 2.8896 - 2.7784 1.00 3246 174 0.1825 0.2448
REMARK 3 10 2.7784 - 2.6825 1.00 3300 149 0.1832 0.2267
REMARK 3 11 2.6825 - 2.5987 1.00 3233 181 0.1901 0.2452
REMARK 3 12 2.5987 - 2.5244 1.00 3280 136 0.1968 0.2228
REMARK 3 13 2.5244 - 2.4579 1.00 3275 151 0.1934 0.2640
REMARK 3 14 2.4579 - 2.3979 1.00 3217 180 0.1956 0.2764
REMARK 3 15 2.3979 - 2.3434 1.00 3239 191 0.1932 0.2379
REMARK 3 16 2.3434 - 2.2936 1.00 3213 173 0.1992 0.2130
REMARK 3 17 2.2936 - 2.2477 1.00 3257 177 0.1950 0.2726
REMARK 3 18 2.2477 - 2.2053 1.00 3202 199 0.2047 0.2705
REMARK 3 19 2.2053 - 2.1659 1.00 3252 158 0.2222 0.2845
REMARK 3 20 2.1659 - 2.1292 1.00 3208 168 0.2249 0.2957
REMARK 3 21 2.1292 - 2.0948 1.00 3237 166 0.2348 0.2863
REMARK 3 22 2.0948 - 2.0626 1.00 3227 162 0.2451 0.2861
REMARK 3 23 2.0626 - 2.0323 1.00 3248 160 0.2444 0.2800
REMARK 3 24 2.0323 - 2.0036 1.00 3241 174 0.2559 0.3212
REMARK 3 25 2.0036 - 1.9765 1.00 3217 176 0.2829 0.3388
REMARK 3 26 1.9765 - 1.9509 1.00 3169 190 0.2943 0.3533
REMARK 3 27 1.9509 - 1.9265 1.00 3238 169 0.3044 0.3663
REMARK 3 28 1.9265 - 1.9033 1.00 3175 172 0.3212 0.3485
REMARK 3 29 1.9033 - 1.8811 1.00 3257 168 0.3415 0.3725
REMARK 3 30 1.8811 - 1.8600 1.00 3198 176 0.3517 0.3740
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 5FY7 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_1290066370.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 23-FEB-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.2
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) : 0.92819
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 : 102989
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.860
REMARK 200 RESOLUTION RANGE LOW (A) : 55.380
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 1.100
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 6.600
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.9000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.86
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.91
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.9
REMARK 200 DATA REDUNDANCY IN SHELL : 5.60
REMARK 200 R MERGE FOR SHELL (I) : 1.38000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.100
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 3ZLI
REMARK 200
REMARK 200 REMARK: NONE
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.67
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.97
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES PH 7.2, 25% PEG3350
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 45.84500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 59.96500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 55.38500
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 59.96500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 45.84500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 55.38500
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000
REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000
REMARK 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A 798
REMARK 465 LEU A 799
REMARK 465 PRO A 800
REMARK 465 THR A 923
REMARK 465 GLN A 924
REMARK 465 HIS A 925
REMARK 465 LYS A 926
REMARK 465 ASP A 927
REMARK 465 HIS A 928
REMARK 465 SER A 929
REMARK 465 ASP A 930
REMARK 465 ASN A 931
REMARK 465 GLU A 932
REMARK 465 SER A 933
REMARK 465 THR A 934
REMARK 465 SER A 935
REMARK 465 SER A 936
REMARK 465 GLU A 937
REMARK 465 ASN A 938
REMARK 465 SER A 939
REMARK 465 GLY A 940
REMARK 465 ARG A 941
REMARK 465 SER A 1266
REMARK 465 SER A 1267
REMARK 465 SER A 1268
REMARK 465 ALA A 1269
REMARK 465 GLU A 1270
REMARK 465 ASN A 1271
REMARK 465 LEU A 1272
REMARK 465 TYR A 1273
REMARK 465 PHE A 1274
REMARK 465 GLN A 1275
REMARK 465 MET B 798
REMARK 465 LEU B 799
REMARK 465 PRO B 800
REMARK 465 LYS B 801
REMARK 465 LYS B 921
REMARK 465 ARG B 922
REMARK 465 THR B 923
REMARK 465 GLN B 924
REMARK 465 HIS B 925
REMARK 465 LYS B 926
REMARK 465 ASP B 927
REMARK 465 HIS B 928
REMARK 465 SER B 929
REMARK 465 ASP B 930
REMARK 465 ASN B 931
REMARK 465 GLU B 932
REMARK 465 SER B 933
REMARK 465 THR B 934
REMARK 465 SER B 935
REMARK 465 SER B 936
REMARK 465 GLU B 937
REMARK 465 ASN B 938
REMARK 465 SER B 939
REMARK 465 GLY B 940
REMARK 465 ARG B 941
REMARK 465 ARG B 942
REMARK 465 ARG B 943
REMARK 465 LYS B 944
REMARK 465 GLY B 945
REMARK 465 TYR B 1273
REMARK 465 PHE B 1274
REMARK 465 GLN B 1275
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 LYS A 801 CG CD CE NZ
REMARK 470 ASP A 802 CG OD1 OD2
REMARK 470 LYS A 803 CG CD CE NZ
REMARK 470 GLN A 826 CG CD OE1 NE2
REMARK 470 LYS A 832 CE NZ
REMARK 470 LYS A 855 CD CE NZ
REMARK 470 GLU A 859 CG CD OE1 OE2
REMARK 470 LYS A 886 CE NZ
REMARK 470 GLU A 892 CG CD OE1 OE2
REMARK 470 GLU A 917 CG CD OE1 OE2
REMARK 470 GLU A 920 CG CD OE1 OE2
REMARK 470 ARG A 922 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 942 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 943 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 962 CD CE NZ
REMARK 470 LYS A1051 CG CD CE NZ
REMARK 470 LYS A1155 CG CD CE NZ
REMARK 470 GLU A1158 CG CD OE1 OE2
REMARK 470 LYS A1169 CE NZ
REMARK 470 ASP A1193 CG OD1 OD2
REMARK 470 LYS A1220 CE NZ
REMARK 470 LYS A1235 CG CD CE NZ
REMARK 470 GLU A1249 CG CD OE1 OE2
REMARK 470 LYS B 803 CD CE NZ
REMARK 470 GLU B 814 CG CD OE1 OE2
REMARK 470 LYS B 816 CG CD CE NZ
REMARK 470 LYS B 846 CE NZ
REMARK 470 LYS B 855 CE NZ
REMARK 470 GLU B 859 CD OE1 OE2
REMARK 470 LYS B 886 CE NZ
REMARK 470 GLU B 892 CG CD OE1 OE2
REMARK 470 ARG B 895 CD NE CZ NH1 NH2
REMARK 470 LYS B 902 CE NZ
REMARK 470 ARG B 916 CZ NH1 NH2
REMARK 470 GLU B 917 CD OE1 OE2
REMARK 470 LYS B 965 CE NZ
REMARK 470 LYS B1155 CG CD CE NZ
REMARK 470 GLU B1249 CG CD OE1 OE2
REMARK 470 GLN B1253 CG CD OE1 NE2
REMARK 470 LEU B1272 CG CD1 CD2
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT
REMARK 500
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE
REMARK 500 O HOH B 3086 O HOH B 3103 2.06
REMARK 500 O HOH B 3108 O HOH B 3250 2.08
REMARK 500 O HOH A 3032 O HOH A 3206 2.10
REMARK 500 O HOH B 3286 O HOH B 3332 2.12
REMARK 500 OE1 GLN A 1253 NE2 GLN A 1257 2.13
REMARK 500 O HOH A 3133 O HOH A 3134 2.14
REMARK 500 O HOH A 3360 O HOH A 3363 2.16
REMARK 500 OD2 ASP B 1256 O HOH B 3345 2.17
REMARK 500 O HOH A 3205 O HOH A 3388 2.18
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 ASN A 861 78.34 -153.26
REMARK 500 ALA A 876 -119.55 42.52
REMARK 500 SER A 893 69.83 -154.31
REMARK 500 LYS A 921 -162.23 61.21
REMARK 500 MET A 997 -63.22 -108.06
REMARK 500 ASN A1018 28.48 46.68
REMARK 500 ASN A1208 -67.65 73.50
REMARK 500 ASN B 861 74.23 -151.16
REMARK 500 ALA B 876 -119.74 47.19
REMARK 500 MET B 997 -60.94 -109.73
REMARK 500 ILE B1201 -62.31 -94.37
REMARK 500 ASN B1208 -68.83 75.00
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 A3298 DISTANCE = 5.87 ANGSTROMS
REMARK 525 HOH A3348 DISTANCE = 6.21 ANGSTROMS
REMARK 525 HOH B3310 DISTANCE = 6.21 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 MN A2266 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A1014 NE2
REMARK 620 2 GLU A1016 OE2 91.1
REMARK 620 3 HIS A1094 NE2 80.5 88.1
REMARK 620 4 SIN A2267 O3 92.2 173.3 98.1
REMARK 620 5 HOH A3154 O 90.3 88.5 170.2 85.6
REMARK 620 6 HOH A3163 O 175.3 91.8 103.2 84.6 86.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A4002 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A1199 SG
REMARK 620 2 CYS A1202 SG 108.1
REMARK 620 3 CYS A1226 SG 110.8 113.3
REMARK 620 4 CYS A1229 SG 110.1 110.7 103.8
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MN B2273 MN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B1014 NE2
REMARK 620 2 GLU B1016 OE2 88.7
REMARK 620 3 HIS B1094 NE2 82.3 88.6
REMARK 620 4 SIN B2274 O1 96.0 175.1 93.3
REMARK 620 5 HOH B3154 O 91.1 88.9 173.0 89.7
REMARK 620 6 HOH B3162 O 174.7 87.6 101.4 87.6 85.1
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B4002 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B1199 SG
REMARK 620 2 CYS B1202 SG 110.4
REMARK 620 3 CYS B1226 SG 112.8 113.0
REMARK 620 4 CYS B1229 SG 105.2 110.5 104.4
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 4002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 4002
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN B 2273
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MN A 2266
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SIN B 2274
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SIN A 2267
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 2275
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 2268
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 2269
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 2270
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 2271
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 2272
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 2276
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 2277
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 2278
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 2273
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 2279
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 2274
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 2280
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 2281
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 2282
REMARK 800
REMARK 800 SITE_IDENTIFIER: CC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 2283
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: 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: 5FYZ RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF HUMAN JARID1B IN
REMARK 900 COMPLEX WITH N10063A
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
DBREF 5FY7 A 799 1268 UNP O14607 UTY_HUMAN 878 1347
DBREF 5FY7 B 799 1268 UNP O14607 UTY_HUMAN 878 1347
SEQADV 5FY7 MET A 798 UNP O14607 EXPRESSION TAG
SEQADV 5FY7 ALA A 1269 UNP O14607 EXPRESSION TAG
SEQADV 5FY7 GLU A 1270 UNP O14607 EXPRESSION TAG
SEQADV 5FY7 ASN A 1271 UNP O14607 EXPRESSION TAG
SEQADV 5FY7 LEU A 1272 UNP O14607 EXPRESSION TAG
SEQADV 5FY7 TYR A 1273 UNP O14607 EXPRESSION TAG
SEQADV 5FY7 PHE A 1274 UNP O14607 EXPRESSION TAG
SEQADV 5FY7 GLN A 1275 UNP O14607 EXPRESSION TAG
SEQADV 5FY7 MET B 798 UNP O14607 EXPRESSION TAG
SEQADV 5FY7 ALA B 1269 UNP O14607 EXPRESSION TAG
SEQADV 5FY7 GLU B 1270 UNP O14607 EXPRESSION TAG
SEQADV 5FY7 ASN B 1271 UNP O14607 EXPRESSION TAG
SEQADV 5FY7 LEU B 1272 UNP O14607 EXPRESSION TAG
SEQADV 5FY7 TYR B 1273 UNP O14607 EXPRESSION TAG
SEQADV 5FY7 PHE B 1274 UNP O14607 EXPRESSION TAG
SEQADV 5FY7 GLN B 1275 UNP O14607 EXPRESSION TAG
SEQRES 1 A 478 MET LEU PRO LYS ASP LYS LEU ASN PRO PRO THR PRO SER
SEQRES 2 A 478 ILE TYR LEU GLU ASN LYS ARG ASP ALA PHE PHE PRO PRO
SEQRES 3 A 478 LEU HIS GLN PHE CYS THR ASN PRO LYS ASN PRO VAL THR
SEQRES 4 A 478 VAL ILE ARG GLY LEU ALA GLY ALA LEU LYS LEU ASP LEU
SEQRES 5 A 478 GLY LEU PHE SER THR LYS THR LEU VAL GLU ALA ASN ASN
SEQRES 6 A 478 GLU HIS MET VAL GLU VAL ARG THR GLN LEU LEU GLN PRO
SEQRES 7 A 478 ALA ASP GLU ASN TRP ASP PRO THR GLY THR LYS LYS ILE
SEQRES 8 A 478 TRP ARG CYS GLU SER ASN ARG SER HIS THR THR ILE ALA
SEQRES 9 A 478 LYS TYR ALA GLN TYR GLN ALA SER SER PHE GLN GLU SER
SEQRES 10 A 478 LEU ARG GLU GLU ASN GLU LYS ARG THR GLN HIS LYS ASP
SEQRES 11 A 478 HIS SER ASP ASN GLU SER THR SER SER GLU ASN SER GLY
SEQRES 12 A 478 ARG ARG ARG LYS GLY PRO PHE LYS THR ILE LYS PHE GLY
SEQRES 13 A 478 THR ASN ILE ASP LEU SER ASP ASN LYS LYS TRP LYS LEU
SEQRES 14 A 478 GLN LEU HIS GLU LEU THR LYS LEU PRO ALA PHE ALA ARG
SEQRES 15 A 478 VAL VAL SER ALA GLY ASN LEU LEU THR HIS VAL GLY HIS
SEQRES 16 A 478 THR ILE LEU GLY MET ASN THR VAL GLN LEU TYR MET LYS
SEQRES 17 A 478 VAL PRO GLY SER ARG THR PRO GLY HIS GLN GLU ASN ASN
SEQRES 18 A 478 ASN PHE CYS SER VAL ASN ILE ASN ILE GLY PRO GLY ASP
SEQRES 19 A 478 CYS GLU TRP PHE VAL VAL PRO GLU ASP TYR TRP GLY VAL
SEQRES 20 A 478 LEU ASN ASP PHE CYS GLU LYS ASN ASN LEU ASN PHE LEU
SEQRES 21 A 478 MET SER SER TRP TRP PRO ASN LEU GLU ASP LEU TYR GLU
SEQRES 22 A 478 ALA ASN VAL PRO VAL TYR ARG PHE ILE GLN ARG PRO GLY
SEQRES 23 A 478 ASP LEU VAL TRP ILE ASN ALA GLY THR VAL HIS TRP VAL
SEQRES 24 A 478 GLN ALA VAL GLY TRP CYS ASN ASN ILE ALA TRP ASN VAL
SEQRES 25 A 478 GLY PRO LEU THR ALA CYS GLN TYR LYS LEU ALA VAL GLU
SEQRES 26 A 478 ARG TYR GLU TRP ASN LYS LEU LYS SER VAL LYS SER PRO
SEQRES 27 A 478 VAL PRO MET VAL HIS LEU SER TRP ASN MET ALA ARG ASN
SEQRES 28 A 478 ILE LYS VAL SER ASP PRO LYS LEU PHE GLU MET ILE LYS
SEQRES 29 A 478 TYR CYS LEU LEU LYS ILE LEU LYS GLN TYR GLN THR LEU
SEQRES 30 A 478 ARG GLU ALA LEU VAL ALA ALA GLY LYS GLU VAL ILE TRP
SEQRES 31 A 478 HIS GLY ARG THR ASN ASP GLU PRO ALA HIS TYR CYS SER
SEQRES 32 A 478 ILE CYS GLU VAL GLU VAL PHE ASN LEU LEU PHE VAL THR
SEQRES 33 A 478 ASN GLU SER ASN THR GLN LYS THR TYR ILE VAL HIS CYS
SEQRES 34 A 478 HIS ASP CYS ALA ARG LYS THR SER LYS SER LEU GLU ASN
SEQRES 35 A 478 PHE VAL VAL LEU GLU GLN TYR LYS MET GLU ASP LEU ILE
SEQRES 36 A 478 GLN VAL TYR ASP GLN PHE THR LEU ALA LEU SER LEU SER
SEQRES 37 A 478 SER SER SER ALA GLU ASN LEU TYR PHE GLN
SEQRES 1 B 478 MET LEU PRO LYS ASP LYS LEU ASN PRO PRO THR PRO SER
SEQRES 2 B 478 ILE TYR LEU GLU ASN LYS ARG ASP ALA PHE PHE PRO PRO
SEQRES 3 B 478 LEU HIS GLN PHE CYS THR ASN PRO LYS ASN PRO VAL THR
SEQRES 4 B 478 VAL ILE ARG GLY LEU ALA GLY ALA LEU LYS LEU ASP LEU
SEQRES 5 B 478 GLY LEU PHE SER THR LYS THR LEU VAL GLU ALA ASN ASN
SEQRES 6 B 478 GLU HIS MET VAL GLU VAL ARG THR GLN LEU LEU GLN PRO
SEQRES 7 B 478 ALA ASP GLU ASN TRP ASP PRO THR GLY THR LYS LYS ILE
SEQRES 8 B 478 TRP ARG CYS GLU SER ASN ARG SER HIS THR THR ILE ALA
SEQRES 9 B 478 LYS TYR ALA GLN TYR GLN ALA SER SER PHE GLN GLU SER
SEQRES 10 B 478 LEU ARG GLU GLU ASN GLU LYS ARG THR GLN HIS LYS ASP
SEQRES 11 B 478 HIS SER ASP ASN GLU SER THR SER SER GLU ASN SER GLY
SEQRES 12 B 478 ARG ARG ARG LYS GLY PRO PHE LYS THR ILE LYS PHE GLY
SEQRES 13 B 478 THR ASN ILE ASP LEU SER ASP ASN LYS LYS TRP LYS LEU
SEQRES 14 B 478 GLN LEU HIS GLU LEU THR LYS LEU PRO ALA PHE ALA ARG
SEQRES 15 B 478 VAL VAL SER ALA GLY ASN LEU LEU THR HIS VAL GLY HIS
SEQRES 16 B 478 THR ILE LEU GLY MET ASN THR VAL GLN LEU TYR MET LYS
SEQRES 17 B 478 VAL PRO GLY SER ARG THR PRO GLY HIS GLN GLU ASN ASN
SEQRES 18 B 478 ASN PHE CYS SER VAL ASN ILE ASN ILE GLY PRO GLY ASP
SEQRES 19 B 478 CYS GLU TRP PHE VAL VAL PRO GLU ASP TYR TRP GLY VAL
SEQRES 20 B 478 LEU ASN ASP PHE CYS GLU LYS ASN ASN LEU ASN PHE LEU
SEQRES 21 B 478 MET SER SER TRP TRP PRO ASN LEU GLU ASP LEU TYR GLU
SEQRES 22 B 478 ALA ASN VAL PRO VAL TYR ARG PHE ILE GLN ARG PRO GLY
SEQRES 23 B 478 ASP LEU VAL TRP ILE ASN ALA GLY THR VAL HIS TRP VAL
SEQRES 24 B 478 GLN ALA VAL GLY TRP CYS ASN ASN ILE ALA TRP ASN VAL
SEQRES 25 B 478 GLY PRO LEU THR ALA CYS GLN TYR LYS LEU ALA VAL GLU
SEQRES 26 B 478 ARG TYR GLU TRP ASN LYS LEU LYS SER VAL LYS SER PRO
SEQRES 27 B 478 VAL PRO MET VAL HIS LEU SER TRP ASN MET ALA ARG ASN
SEQRES 28 B 478 ILE LYS VAL SER ASP PRO LYS LEU PHE GLU MET ILE LYS
SEQRES 29 B 478 TYR CYS LEU LEU LYS ILE LEU LYS GLN TYR GLN THR LEU
SEQRES 30 B 478 ARG GLU ALA LEU VAL ALA ALA GLY LYS GLU VAL ILE TRP
SEQRES 31 B 478 HIS GLY ARG THR ASN ASP GLU PRO ALA HIS TYR CYS SER
SEQRES 32 B 478 ILE CYS GLU VAL GLU VAL PHE ASN LEU LEU PHE VAL THR
SEQRES 33 B 478 ASN GLU SER ASN THR GLN LYS THR TYR ILE VAL HIS CYS
SEQRES 34 B 478 HIS ASP CYS ALA ARG LYS THR SER LYS SER LEU GLU ASN
SEQRES 35 B 478 PHE VAL VAL LEU GLU GLN TYR LYS MET GLU ASP LEU ILE
SEQRES 36 B 478 GLN VAL TYR ASP GLN PHE THR LEU ALA LEU SER LEU SER
SEQRES 37 B 478 SER SER SER ALA GLU ASN LEU TYR PHE GLN
HET MN A2266 1
HET SIN A2267 8
HET EDO A2268 4
HET EDO A2269 4
HET EDO A2270 4
HET EDO A2271 4
HET EDO A2272 4
HET EDO A2273 4
HET EDO A2274 4
HET ZN A4002 1
HET MN B2273 1
HET SIN B2274 8
HET EDO B2275 4
HET EDO B2276 4
HET EDO B2277 4
HET EDO B2278 4
HET EDO B2279 4
HET EDO B2280 4
HET EDO B2281 4
HET EDO B2282 4
HET EDO B2283 4
HET ZN B4002 1
HETNAM MN MANGANESE (II) ION
HETNAM SIN SUCCINIC ACID
HETNAM EDO 1,2-ETHANEDIOL
HETNAM ZN ZINC ION
HETSYN EDO ETHYLENE GLYCOL
FORMUL 3 MN 2(MN 2+)
FORMUL 4 SIN 2(C4 H6 O4)
FORMUL 5 EDO 16(C2 H6 O2)
FORMUL 12 ZN 2(ZN 2+)
FORMUL 25 HOH *745(H2 O)
HELIX 1 1 LYS A 801 ASN A 805 5 5
HELIX 2 2 ASN A 815 PHE A 821 1 7
HELIX 3 3 PHE A 821 ASN A 830 1 10
HELIX 4 4 GLY A 840 LYS A 846 1 7
HELIX 5 5 ASP A 848 PHE A 852 5 5
HELIX 6 6 SER A 853 ASN A 861 1 9
HELIX 7 7 ILE A 900 ASN A 919 1 20
HELIX 8 8 TRP A 964 LEU A 971 1 8
HELIX 9 9 THR A 972 LEU A 974 5 3
HELIX 10 10 PRO A 975 ARG A 979 5 5
HELIX 11 11 ASN A 985 VAL A 990 1 6
HELIX 12 12 GLU A 1016 PHE A 1020 5 5
HELIX 13 13 PRO A 1038 ASP A 1040 5 3
HELIX 14 14 TYR A 1041 ASN A 1052 1 12
HELIX 15 15 ASN A 1064 ALA A 1071 1 8
HELIX 16 16 THR A 1113 LYS A 1130 1 18
HELIX 17 17 PRO A 1137 ILE A 1149 1 13
HELIX 18 18 ASP A 1153 ALA A 1181 1 29
HELIX 19 19 ASN A 1214 GLN A 1219 1 6
HELIX 20 20 CYS A 1226 SER A 1234 1 9
HELIX 21 21 LYS A 1247 PHE A 1258 1 12
HELIX 22 22 ASN B 815 PHE B 820 1 6
HELIX 23 23 PRO B 822 ASN B 830 1 9
HELIX 24 24 GLY B 840 LYS B 846 1 7
HELIX 25 25 ASP B 848 PHE B 852 5 5
HELIX 26 26 SER B 853 ASN B 861 1 9
HELIX 27 27 ILE B 900 GLU B 920 1 21
HELIX 28 28 TRP B 964 LEU B 971 1 8
HELIX 29 29 THR B 972 LEU B 974 5 3
HELIX 30 30 PRO B 975 ARG B 979 5 5
HELIX 31 31 ASN B 985 VAL B 990 1 6
HELIX 32 32 GLU B 1016 PHE B 1020 5 5
HELIX 33 33 PRO B 1038 ASP B 1040 5 3
HELIX 34 34 TYR B 1041 LYS B 1051 1 11
HELIX 35 35 ASN B 1064 ALA B 1071 1 8
HELIX 36 36 THR B 1113 LYS B 1130 1 18
HELIX 37 37 PRO B 1137 ASN B 1148 1 12
HELIX 38 38 ASP B 1153 ALA B 1181 1 29
HELIX 39 39 ASN B 1214 GLN B 1219 1 6
HELIX 40 40 CYS B 1226 SER B 1234 1 9
HELIX 41 41 LYS B 1247 GLN B 1257 1 11
SHEET 1 AA 9 SER A 810 TYR A 812 0
SHEET 2 AA 9 VAL A 835 ARG A 839 1 O VAL A 837 N ILE A 811
SHEET 3 AA 9 LEU A1085 ILE A1088 -1 O LEU A1085 N ILE A 838
SHEET 4 AA 9 CYS A1021 PRO A1029 -1 O SER A1022 N ILE A1088
SHEET 5 AA 9 CYS A1102 VAL A1109 -1 O ASN A1103 N ILE A1027
SHEET 6 AA 9 GLN A1001 MET A1004 -1 O GLN A1001 N ALA A1106
SHEET 7 AA 9 THR A 949 ASP A 957 -1 O GLY A 953 N MET A1004
SHEET 8 AA 9 MET A 865 LEU A 872 -1 O GLU A 867 N THR A 954
SHEET 9 AA 9 ASN A 894 THR A 899 -1 O ASN A 894 N THR A 870
SHEET 1 AB 4 ARG A1010 HIS A1014 0
SHEET 2 AB 4 VAL A1093 ALA A1098 -1 O HIS A1094 N HIS A1014
SHEET 3 AB 4 CYS A1032 VAL A1037 -1 O GLU A1033 N GLN A1097
SHEET 4 AB 4 TYR A1076 GLN A1080 -1 O TYR A1076 N VAL A1036
SHEET 1 AC 3 VAL A1185 TRP A1187 0
SHEET 2 AC 3 PHE A1240 GLU A1244 1 O VAL A1242 N ILE A1186
SHEET 3 AC 3 LEU A1209 THR A1213 -1 O LEU A1210 N LEU A1243
SHEET 1 AD 2 HIS A1197 TYR A1198 0
SHEET 2 AD 2 GLU A1205 VAL A1206 -1 O VAL A1206 N HIS A1197
SHEET 1 BA 9 SER B 810 TYR B 812 0
SHEET 2 BA 9 VAL B 835 ARG B 839 1 O VAL B 837 N ILE B 811
SHEET 3 BA 9 LEU B1085 ILE B1088 -1 O LEU B1085 N ILE B 838
SHEET 4 BA 9 CYS B1021 PRO B1029 -1 O SER B1022 N ILE B1088
SHEET 5 BA 9 CYS B1102 VAL B1109 -1 O ASN B1103 N ILE B1027
SHEET 6 BA 9 GLN B1001 LYS B1005 -1 O GLN B1001 N ALA B1106
SHEET 7 BA 9 THR B 949 ASP B 957 -1 O GLY B 953 N MET B1004
SHEET 8 BA 9 MET B 865 LEU B 872 -1 O GLU B 867 N THR B 954
SHEET 9 BA 9 SER B 893 THR B 899 -1 O ASN B 894 N THR B 870
SHEET 1 BB 4 ARG B1010 HIS B1014 0
SHEET 2 BB 4 VAL B1093 ALA B1098 -1 O HIS B1094 N HIS B1014
SHEET 3 BB 4 CYS B1032 VAL B1037 -1 O GLU B1033 N GLN B1097
SHEET 4 BB 4 TYR B1076 GLN B1080 -1 O TYR B1076 N VAL B1036
SHEET 1 BC 2 ILE B1149 VAL B1151 0
SHEET 2 BC 2 ALA B1269 ASN B1271 -1 O GLU B1270 N LYS B1150
SHEET 1 BD 3 VAL B1185 TRP B1187 0
SHEET 2 BD 3 PHE B1240 GLU B1244 1 O VAL B1242 N ILE B1186
SHEET 3 BD 3 LEU B1209 THR B1213 -1 O LEU B1210 N LEU B1243
SHEET 1 BE 2 HIS B1197 TYR B1198 0
SHEET 2 BE 2 GLU B1205 VAL B1206 -1 O VAL B1206 N HIS B1197
LINK NE2 HIS A1014 MN MN A2266 1555 1555 2.37
LINK OE2 GLU A1016 MN MN A2266 1555 1555 2.16
LINK NE2 HIS A1094 MN MN A2266 1555 1555 2.35
LINK SG CYS A1199 ZN ZN A4002 1555 1555 2.22
LINK SG CYS A1202 ZN ZN A4002 1555 1555 2.35
LINK SG CYS A1226 ZN ZN A4002 1555 1555 2.29
LINK SG CYS A1229 ZN ZN A4002 1555 1555 2.44
LINK MN MN A2266 O3 SIN A2267 1555 1555 2.14
LINK MN MN A2266 O HOH A3154 1555 1555 2.18
LINK MN MN A2266 O HOH A3163 1555 1555 2.26
LINK NE2 HIS B1014 MN MN B2273 1555 1555 2.38
LINK OE2 GLU B1016 MN MN B2273 1555 1555 2.21
LINK NE2 HIS B1094 MN MN B2273 1555 1555 2.37
LINK SG CYS B1199 ZN ZN B4002 1555 1555 2.33
LINK SG CYS B1202 ZN ZN B4002 1555 1555 2.40
LINK SG CYS B1226 ZN ZN B4002 1555 1555 2.28
LINK SG CYS B1229 ZN ZN B4002 1555 1555 2.42
LINK MN MN B2273 O1 SIN B2274 1555 1555 2.19
LINK MN MN B2273 O HOH B3154 1555 1555 2.27
LINK MN MN B2273 O HOH B3162 1555 1555 2.28
CISPEP 1 GLY A 945 PRO A 946 0 -2.20
CISPEP 2 GLY A 1028 PRO A 1029 0 7.47
CISPEP 3 GLY B 1028 PRO B 1029 0 6.74
SITE 1 AC1 4 CYS A1199 CYS A1202 CYS A1226 CYS A1229
SITE 1 AC2 4 CYS B1199 CYS B1202 CYS B1226 CYS B1229
SITE 1 AC3 6 HIS B1014 GLU B1016 HIS B1094 SIN B2274
SITE 2 AC3 6 HOH B3154 HOH B3162
SITE 1 AC4 6 HIS A1014 GLU A1016 HIS A1094 SIN A2267
SITE 2 AC4 6 HOH A3154 HOH A3163
SITE 1 AC5 9 LYS B1005 THR B1011 HIS B1014 ASN B1024
SITE 2 AC5 9 HIS B1094 ASN B1104 MN B2273 HOH B3148
SITE 3 AC5 9 HOH B3162
SITE 1 AC6 11 LYS A1005 THR A1011 HIS A1014 ASN A1024
SITE 2 AC6 11 TRP A1034 HIS A1094 ASN A1104 MN A2266
SITE 3 AC6 11 HOH A3148 HOH A3154 HOH A3163
SITE 1 AC7 5 ILE B 888 TRP B 889 ARG B 890 HOH B3077
SITE 2 AC7 5 HOH B3350
SITE 1 AC8 7 SER A 853 THR A 854 GLN A 907 PRO A1029
SITE 2 AC8 7 EDO A2269 EDO A2273 HOH A3043
SITE 1 AC9 3 EDO A2268 HOH A3085 HOH A3387
SITE 1 BC1 4 ARG A1077 HOH A3003 ASN B 919 GLU B 920
SITE 1 BC2 4 HIS A1188 HIS A1197 TYR A1222 VAL A1224
SITE 1 BC3 7 GLY A 840 ALA A 842 GLY A 843 PRO A1082
SITE 2 BC3 7 GLY A1083 ASP A1084 HOH A3388
SITE 1 BC4 4 LYS A 816 VAL B1044 ASP B1047 PHE B1048
SITE 1 BC5 7 GLN B 907 PHE B 911 TRP B1101 EDO B2278
SITE 2 BC5 7 HOH B3092 HOH B3352 HOH B3353
SITE 1 BC6 5 THR B 854 GLN B 907 PRO B1029 EDO B2277
SITE 2 BC6 5 HOH B3035
SITE 1 BC7 5 LEU A 849 GLY A 850 SER A 853 GLY A1028
SITE 2 BC7 5 EDO A2268
SITE 1 BC8 6 LEU B 971 THR B 972 ARG B 979 VAL B 980
SITE 2 BC8 6 VAL B 981 HOH B3137
SITE 1 BC9 8 GLY A 996 TYR A1003 GLU A1016 ALA A1106
SITE 2 BC9 8 TRP A1107 ASN A1108 HOH A3145 HOH A3154
SITE 1 CC1 5 HIS B 864 ASP B 957 ASP B 960 LYS B 963
SITE 2 CC1 5 HOH B3110
SITE 1 CC2 6 LYS B1128 SER B1131 CYS B1202 VAL B1204
SITE 2 CC2 6 HOH B3236 HOH B3355
SITE 1 CC3 10 GLY B 996 GLN B1001 TYR B1003 GLU B1016
SITE 2 CC3 10 SER B1022 TRP B1107 ASN B1108 HOH B3147
SITE 3 CC3 10 HOH B3154 HOH B3356
SITE 1 CC4 4 ARG A1081 SER B 914 GLU B 918 TRP B1101
CRYST1 91.690 110.770 119.930 90.00 90.00 90.00 P 21 21 21 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 0.010906 0.000000 0.000000 0.00000
SCALE2 0.000000 0.009028 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008338 0.00000
(ATOM LINES ARE NOT SHOWN.)
END