HEADER OXIDOREDUCTASE 14-DEC-15 5FBJ
TITLE COMPLEX STRUCTURE OF JMJD5 AND SUBSTRATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LYSINE-SPECIFIC DEMETHYLASE 8;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: JMJC DOMAIN-CONTAINING PROTEIN 5,JUMONJI DOMAIN-CONTAINING
COMPND 5 PROTEIN 5;
COMPND 6 EC: 1.14.11.27;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: KDM8, JMJD5;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PGEX4T1
KEYWDS HISTONE ENZYME, OXIDOREDUCTASE
EXPDTA X-RAY DIFFRACTION
AUTHOR H.L.LIU,Y.WANG,C.WANG,G.Y.ZHANG
REVDAT 2 27-SEP-23 5FBJ 1 REMARK
REVDAT 1 14-DEC-16 5FBJ 0
JRNL AUTH H.L.LIU,Y.WANG,C.WANG,S.D.DAI,G.Y.ZHANG
JRNL TITL TO BE PUBLISHED
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.42 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.9_1692
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) : 2.42
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.98
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350
REMARK 3 COMPLETENESS FOR RANGE (%) : 77.2
REMARK 3 NUMBER OF REFLECTIONS : 7775
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.193
REMARK 3 R VALUE (WORKING SET) : 0.190
REMARK 3 FREE R VALUE : 0.246
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.780
REMARK 3 FREE R VALUE TEST SET COUNT : 372
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 38.9800 - 3.4900 0.70 2303 120 0.1641 0.2267
REMARK 3 2 3.4900 - 2.7704 0.81 2571 116 0.1944 0.2280
REMARK 3 3 2.7704 - 2.4202 0.81 2529 136 0.2399 0.3101
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) : 0.260
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.070
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 : 0.004 2012
REMARK 3 ANGLE : 0.925 2744
REMARK 3 CHIRALITY : 0.038 288
REMARK 3 PLANARITY : 0.004 358
REMARK 3 DIHEDRAL : 16.546 740
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5FBJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-DEC-15.
REMARK 100 THE DEPOSITION ID IS D_1000216325.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-SEP-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7.0
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : N
REMARK 200 RADIATION SOURCE : ROTATING ANODE
REMARK 200 BEAMLINE : NULL
REMARK 200 X-RAY GENERATOR MODEL : OTHER
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.5418
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : IMAGE PLATE
REMARK 200 DETECTOR MANUFACTURER : RIGAKU RAXIS IV++
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 7775
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400
REMARK 200 RESOLUTION RANGE LOW (A) : 38.975
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 77.2
REMARK 200 DATA REDUNDANCY : 6.700
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 2.0000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : NULL
REMARK 200 COMPLETENESS FOR SHELL (%) : NULL
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: 4QU1
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.49
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.30
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG3350 HEPEPS-NA, EVAPORATION,
REMARK 280 TEMPERATURE 281K
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 24.76950
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 38.97500
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 32.52600
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 38.97500
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 24.76950
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 32.52600
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
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 TOTAL BURIED SURFACE AREA: 470 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 11320 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -41.0 KCAL/MOL
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 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 ARG A 196 CZ NH1 NH2
REMARK 470 GLU A 246 CG CD OE1 OE2
REMARK 470 GLU A 247 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 O HOH A 654 O HOH A 667 1.85
REMARK 500 O HIS A 355 ND1 HIS A 358 1.99
REMARK 500 OD2 ASP A 369 O HOH A 601 2.07
REMARK 500 O GLN A 325 O HOH A 602 2.15
REMARK 500 O HOH A 680 O HOH A 688 2.16
REMARK 500 NE2 GLN A 198 O HOH A 603 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 PHE A 199 -43.61 -135.90
REMARK 500 GLU A 247 41.04 -87.85
REMARK 500 ILE A 263 -60.07 -130.82
REMARK 500 ASN A 265 53.92 -99.13
REMARK 500 GLU A 266 77.06 41.63
REMARK 500 HIS A 355 -59.89 70.06
REMARK 500 ASN A 367 70.78 -155.45
REMARK 500
REMARK 500 REMARK: NULL
REMARK 615
REMARK 615 ZERO OCCUPANCY ATOM
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 615 M RES C SSEQI
REMARK 615 NMM A 502
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 ZN A 503 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 321 NE2
REMARK 620 2 ASP A 323 OD2 105.6
REMARK 620 3 HIS A 400 NE2 85.4 83.2
REMARK 620 4 AKG A 501 O2 162.5 91.8 97.9
REMARK 620 5 AKG A 501 O5 84.2 170.2 98.9 78.4
REMARK 620 N 1 2 3 4
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue AKG A 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NMM A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 503
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4QU1 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN JMJD5 JMJ-C DOMAIN
DBREF 5FBJ A 183 416 UNP Q8N371 KDM8_HUMAN 183 416
SEQADV 5FBJ GLY A 181 UNP Q8N371 EXPRESSION TAG
SEQADV 5FBJ SER A 182 UNP Q8N371 EXPRESSION TAG
SEQRES 1 A 236 GLY SER THR VAL PRO ARG LEU HIS ARG PRO SER LEU GLN
SEQRES 2 A 236 HIS PHE ARG GLU GLN PHE LEU VAL PRO GLY ARG PRO VAL
SEQRES 3 A 236 ILE LEU LYS GLY VAL ALA ASP HIS TRP PRO CYS MET GLN
SEQRES 4 A 236 LYS TRP SER LEU GLU TYR ILE GLN GLU ILE ALA GLY CYS
SEQRES 5 A 236 ARG THR VAL PRO VAL GLU VAL GLY SER ARG TYR THR ASP
SEQRES 6 A 236 GLU GLU TRP SER GLN THR LEU MET THR VAL ASN GLU PHE
SEQRES 7 A 236 ILE SER LYS TYR ILE VAL ASN GLU PRO ARG ASP VAL GLY
SEQRES 8 A 236 TYR LEU ALA GLN HIS GLN LEU PHE ASP GLN ILE PRO GLU
SEQRES 9 A 236 LEU LYS GLN ASP ILE SER ILE PRO ASP TYR CYS SER LEU
SEQRES 10 A 236 GLY ASP GLY GLU GLU GLU GLU ILE THR ILE ASN ALA TRP
SEQRES 11 A 236 PHE GLY PRO GLN GLY THR ILE SER PRO LEU HIS GLN ASP
SEQRES 12 A 236 PRO GLN GLN ASN PHE LEU VAL GLN VAL MET GLY ARG LYS
SEQRES 13 A 236 TYR ILE ARG LEU TYR SER PRO GLN GLU SER GLY ALA LEU
SEQRES 14 A 236 TYR PRO HIS ASP THR HIS LEU LEU HIS ASN THR SER GLN
SEQRES 15 A 236 VAL ASP VAL GLU ASN PRO ASP LEU GLU LYS PHE PRO LYS
SEQRES 16 A 236 PHE ALA LYS ALA PRO PHE LEU SER CYS ILE LEU SER PRO
SEQRES 17 A 236 GLY GLU ILE LEU PHE ILE PRO VAL LYS TYR TRP HIS TYR
SEQRES 18 A 236 VAL ARG ALA LEU ASP LEU SER PHE SER VAL SER PHE TRP
SEQRES 19 A 236 TRP SER
HET AKG A 501 10
HET NMM A 502 13
HET ZN A 503 1
HETNAM AKG 2-OXOGLUTARIC ACID
HETNAM NMM (2S)-2-AMINO-5-[(N-METHYLCARBAMIMIDOYL)AMINO]PENTANOIC
HETNAM 2 NMM ACID
HETNAM ZN ZINC ION
HETSYN NMM L-NMMA
FORMUL 2 AKG C5 H6 O5
FORMUL 3 NMM C7 H16 N4 O2
FORMUL 4 ZN ZN 2+
FORMUL 5 HOH *90(H2 O)
HELIX 1 AA1 SER A 191 PHE A 199 1 9
HELIX 2 AA2 PRO A 216 TRP A 221 1 6
HELIX 3 AA3 SER A 222 GLY A 231 1 10
HELIX 4 AA4 VAL A 255 ILE A 263 1 9
HELIX 5 AA5 GLN A 277 ILE A 282 1 6
HELIX 6 AA6 ILE A 282 GLN A 287 1 6
HELIX 7 AA7 PRO A 292 GLY A 298 5 7
HELIX 8 AA8 GLU A 301 ILE A 305 5 5
HELIX 9 AA9 SER A 342 TYR A 350 5 9
HELIX 10 AB1 PHE A 373 ALA A 377 5 5
SHEET 1 AA1 5 SER A 182 THR A 183 0
SHEET 2 AA1 5 LEU A 382 LEU A 386 1 O SER A 383 N SER A 182
SHEET 3 AA1 5 LYS A 336 TYR A 341 -1 N LYS A 336 O LEU A 386
SHEET 4 AA1 5 TRP A 399 ALA A 404 -1 O ARG A 403 N TYR A 337
SHEET 5 AA1 5 ILE A 317 HIS A 321 -1 N SER A 318 O VAL A 402
SHEET 1 AA2 9 ARG A 186 HIS A 188 0
SHEET 2 AA2 9 VAL A 206 LYS A 209 1 O LYS A 209 N LEU A 187
SHEET 3 AA2 9 ILE A 391 ILE A 394 -1 O PHE A 393 N VAL A 206
SHEET 4 AA2 9 GLN A 326 MET A 333 -1 N ASN A 327 O ILE A 394
SHEET 5 AA2 9 SER A 408 TRP A 415 -1 O VAL A 411 N VAL A 330
SHEET 6 AA2 9 THR A 306 GLY A 312 -1 N THR A 306 O TRP A 414
SHEET 7 AA2 9 GLY A 271 HIS A 276 -1 N LEU A 273 O PHE A 311
SHEET 8 AA2 9 THR A 234 VAL A 239 -1 N GLU A 238 O TYR A 272
SHEET 9 AA2 9 SER A 249 THR A 254 -1 O MET A 253 N VAL A 235
LINK NE2 HIS A 321 ZN ZN A 503 1555 1555 2.32
LINK OD2 ASP A 323 ZN ZN A 503 1555 1555 2.01
LINK NE2 HIS A 400 ZN ZN A 503 1555 1555 2.27
LINK O2 AKG A 501 ZN ZN A 503 1555 1555 2.08
LINK O5 AKG A 501 ZN ZN A 503 1555 1555 2.26
SITE 1 AC1 14 TYR A 272 TRP A 310 SER A 318 HIS A 321
SITE 2 AC1 14 ASP A 323 ASN A 327 LYS A 336 HIS A 400
SITE 3 AC1 14 VAL A 402 SER A 412 TRP A 414 NMM A 502
SITE 4 AC1 14 ZN A 503 HOH A 648
SITE 1 AC2 13 GLU A 238 TYR A 243 TYR A 272 GLN A 275
SITE 2 AC2 13 TRP A 310 SER A 318 HIS A 321 ASP A 323
SITE 3 AC2 13 TRP A 414 AKG A 501 ZN A 503 HOH A 632
SITE 4 AC2 13 HOH A 633
SITE 1 AC3 5 HIS A 321 ASP A 323 HIS A 400 AKG A 501
SITE 2 AC3 5 NMM A 502
CRYST1 49.539 65.052 77.950 90.00 90.00 90.00 P 21 21 21 4
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 0.020186 0.000000 0.000000 0.00000
SCALE2 0.000000 0.015372 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012829 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
