HEADER HYDROLASE 23-MAR-17 5NI4
TITLE CRYSTAL STRUCTURE OF HUMAN LTA4H MUTANT E271A IN COMPLEX WITH LTA4
TITLE 2 (CRYSTAL FORM II)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: LEUKOTRIENE A-4 HYDROLASE;
COMPND 3 CHAIN: A, B, C;
COMPND 4 SYNONYM: LTA-4 HYDROLASE,LEUKOTRIENE A(4) HYDROLASE;
COMPND 5 EC: 3.3.2.6;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: LTA4H, LTA4;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: JM101;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PT3MB4
KEYWDS METALLOPEPTIDASE, EPOXIDE HYDROLASE, LEUKOTRIENE A4, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR A.STSIAPANAVA
REVDAT 4 17-JAN-24 5NI4 1 REMARK LINK
REVDAT 3 13-SEP-17 5NI4 1 JRNL
REVDAT 2 06-SEP-17 5NI4 1 JRNL
REVDAT 1 23-AUG-17 5NI4 0
JRNL AUTH A.STSIAPANAVA,B.SAMUELSSON,J.Z.HAEGGSTROM
JRNL TITL CAPTURING LTA4 HYDROLASE IN ACTION: INSIGHTS TO THE
JRNL TITL 2 CHEMISTRY AND DYNAMICS OF CHEMOTACTIC LTB4 SYNTHESIS.
JRNL REF PROC. NATL. ACAD. SCI. V. 114 9689 2017
JRNL REF 2 U.S.A.
JRNL REFN ESSN 1091-6490
JRNL PMID 28827365
JRNL DOI 10.1073/PNAS.1710850114
REMARK 2
REMARK 2 RESOLUTION. 1.90 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.11.1_2575: ???)
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) : 1.90
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.81
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.960
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 152057
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.164
REMARK 3 R VALUE (WORKING SET) : 0.162
REMARK 3 FREE R VALUE : 0.200
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.330
REMARK 3 FREE R VALUE TEST SET COUNT : 8107
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 49.8242 - 5.8856 1.00 4787 272 0.1649 0.1757
REMARK 3 2 5.8856 - 4.6727 1.00 4815 256 0.1185 0.1537
REMARK 3 3 4.6727 - 4.0823 1.00 4812 248 0.1099 0.1416
REMARK 3 4 4.0823 - 3.7092 1.00 4838 279 0.1298 0.1492
REMARK 3 5 3.7092 - 3.4434 1.00 4746 285 0.1345 0.1854
REMARK 3 6 3.4434 - 3.2404 1.00 4791 285 0.1405 0.1719
REMARK 3 7 3.2404 - 3.0782 1.00 4808 276 0.1436 0.1849
REMARK 3 8 3.0782 - 2.9442 1.00 4774 258 0.1476 0.2003
REMARK 3 9 2.9442 - 2.8309 1.00 4822 295 0.1451 0.1931
REMARK 3 10 2.8309 - 2.7332 1.00 4750 269 0.1461 0.1929
REMARK 3 11 2.7332 - 2.6477 1.00 4852 257 0.1462 0.1974
REMARK 3 12 2.6477 - 2.5721 1.00 4775 291 0.1502 0.2018
REMARK 3 13 2.5721 - 2.5043 1.00 4792 268 0.1641 0.2028
REMARK 3 14 2.5043 - 2.4433 1.00 4836 260 0.1664 0.2207
REMARK 3 15 2.4433 - 2.3877 1.00 4788 264 0.1687 0.2169
REMARK 3 16 2.3877 - 2.3369 1.00 4789 272 0.1729 0.2166
REMARK 3 17 2.3369 - 2.2902 1.00 4806 279 0.1769 0.2157
REMARK 3 18 2.2902 - 2.2469 1.00 4777 254 0.2050 0.2688
REMARK 3 19 2.2469 - 2.2068 1.00 4823 281 0.2106 0.2538
REMARK 3 20 2.2068 - 2.1694 1.00 4802 246 0.2080 0.2623
REMARK 3 21 2.1694 - 2.1344 1.00 4828 282 0.2091 0.2396
REMARK 3 22 2.1344 - 2.1016 1.00 4794 272 0.2159 0.2740
REMARK 3 23 2.1016 - 2.0707 1.00 4849 275 0.2274 0.2682
REMARK 3 24 2.0707 - 2.0415 1.00 4747 263 0.2340 0.2531
REMARK 3 25 2.0415 - 2.0139 1.00 4835 266 0.2392 0.2543
REMARK 3 26 2.0139 - 1.9877 1.00 4709 272 0.2483 0.3054
REMARK 3 27 1.9877 - 1.9629 1.00 4800 280 0.2682 0.3185
REMARK 3 28 1.9629 - 1.9392 1.00 4795 264 0.2815 0.3302
REMARK 3 29 1.9392 - 1.9167 1.00 4821 272 0.3116 0.3484
REMARK 3 30 1.9167 - 1.8952 0.99 4789 266 0.3231 0.3642
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) : 0.250
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.220
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 22.08
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 : 0.005 15519
REMARK 3 ANGLE : 0.844 21095
REMARK 3 CHIRALITY : 0.048 2339
REMARK 3 PLANARITY : 0.005 2709
REMARK 3 DIHEDRAL : 17.503 5847
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 9
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND RESI 3:209
REMARK 3 ORIGIN FOR THE GROUP (A): -1.0169 21.8693 -11.1124
REMARK 3 T TENSOR
REMARK 3 T11: 0.2470 T22: 0.1825
REMARK 3 T33: 0.2253 T12: -0.0204
REMARK 3 T13: 0.0041 T23: 0.0038
REMARK 3 L TENSOR
REMARK 3 L11: 0.2170 L22: 0.4398
REMARK 3 L33: 0.4534 L12: -0.0337
REMARK 3 L13: -0.0789 L23: -0.0461
REMARK 3 S TENSOR
REMARK 3 S11: 0.0095 S12: 0.0510 S13: -0.0021
REMARK 3 S21: -0.1204 S22: 0.0144 S23: -0.0412
REMARK 3 S31: -0.1332 S32: 0.0688 S33: 0.0000
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND RESI 210:465
REMARK 3 ORIGIN FOR THE GROUP (A): -16.5836 13.1460 9.8759
REMARK 3 T TENSOR
REMARK 3 T11: 0.1770 T22: 0.1674
REMARK 3 T33: 0.2098 T12: 0.0084
REMARK 3 T13: 0.0006 T23: 0.0036
REMARK 3 L TENSOR
REMARK 3 L11: 0.4042 L22: 0.2467
REMARK 3 L33: 0.4807 L12: -0.0639
REMARK 3 L13: -0.0320 L23: 0.1754
REMARK 3 S TENSOR
REMARK 3 S11: -0.0006 S12: -0.0171 S13: -0.0186
REMARK 3 S21: 0.0395 S22: -0.0227 S23: 0.0270
REMARK 3 S31: 0.0006 S32: -0.0603 S33: 0.0000
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN A AND RESI 466:609
REMARK 3 ORIGIN FOR THE GROUP (A): -8.9941 31.0275 27.6865
REMARK 3 T TENSOR
REMARK 3 T11: 0.2936 T22: 0.2016
REMARK 3 T33: 0.2154 T12: 0.0359
REMARK 3 T13: 0.0033 T23: -0.0252
REMARK 3 L TENSOR
REMARK 3 L11: 0.1596 L22: 0.4988
REMARK 3 L33: 0.3968 L12: -0.0159
REMARK 3 L13: -0.0354 L23: 0.3609
REMARK 3 S TENSOR
REMARK 3 S11: -0.0350 S12: -0.1131 S13: 0.0279
REMARK 3 S21: 0.1138 S22: 0.0735 S23: 0.0428
REMARK 3 S31: -0.2010 S32: 0.0281 S33: 0.0016
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN B AND RESI 2:209
REMARK 3 ORIGIN FOR THE GROUP (A): 15.5153 64.7706 -5.4531
REMARK 3 T TENSOR
REMARK 3 T11: 0.1688 T22: 0.2067
REMARK 3 T33: 0.2000 T12: 0.0427
REMARK 3 T13: 0.0048 T23: 0.0119
REMARK 3 L TENSOR
REMARK 3 L11: 0.3622 L22: 0.3234
REMARK 3 L33: 0.4750 L12: -0.1597
REMARK 3 L13: 0.2478 L23: -0.1868
REMARK 3 S TENSOR
REMARK 3 S11: -0.0218 S12: -0.1310 S13: 0.0282
REMARK 3 S21: -0.0180 S22: 0.0141 S23: -0.0423
REMARK 3 S31: 0.0761 S32: 0.0393 S33: 0.0016
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN B AND RESI 210:465
REMARK 3 ORIGIN FOR THE GROUP (A): -1.7776 59.7246 -26.5050
REMARK 3 T TENSOR
REMARK 3 T11: 0.2388 T22: 0.1709
REMARK 3 T33: 0.1900 T12: -0.0090
REMARK 3 T13: 0.0008 T23: 0.0098
REMARK 3 L TENSOR
REMARK 3 L11: 0.1784 L22: 0.2364
REMARK 3 L33: 0.3958 L12: 0.0841
REMARK 3 L13: -0.1348 L23: -0.1349
REMARK 3 S TENSOR
REMARK 3 S11: -0.0023 S12: 0.0005 S13: 0.0237
REMARK 3 S21: -0.0581 S22: -0.0092 S23: -0.0135
REMARK 3 S31: 0.1141 S32: -0.0350 S33: -0.0001
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN B AND RESI 466:609
REMARK 3 ORIGIN FOR THE GROUP (A): 16.4305 53.2137 -44.4656
REMARK 3 T TENSOR
REMARK 3 T11: 0.4164 T22: 0.2231
REMARK 3 T33: 0.2474 T12: 0.0563
REMARK 3 T13: 0.0740 T23: -0.0036
REMARK 3 L TENSOR
REMARK 3 L11: 0.3839 L22: 0.3028
REMARK 3 L33: 0.2273 L12: -0.0874
REMARK 3 L13: -0.1199 L23: -0.0797
REMARK 3 S TENSOR
REMARK 3 S11: -0.0632 S12: 0.0564 S13: -0.0395
REMARK 3 S21: -0.1900 S22: 0.0081 S23: -0.0701
REMARK 3 S31: 0.1691 S32: 0.0498 S33: -0.0006
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN C AND RESI 2:209
REMARK 3 ORIGIN FOR THE GROUP (A): 58.7741 59.5234 -19.9433
REMARK 3 T TENSOR
REMARK 3 T11: 0.2495 T22: 0.1934
REMARK 3 T33: 0.1980 T12: 0.0158
REMARK 3 T13: -0.0071 T23: 0.0300
REMARK 3 L TENSOR
REMARK 3 L11: 0.5390 L22: 0.3848
REMARK 3 L33: 0.3273 L12: -0.1315
REMARK 3 L13: -0.0803 L23: -0.2511
REMARK 3 S TENSOR
REMARK 3 S11: -0.0018 S12: 0.1477 S13: 0.0408
REMARK 3 S21: -0.0871 S22: 0.0023 S23: -0.0128
REMARK 3 S31: -0.0793 S32: -0.0160 S33: -0.0000
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN C AND RESI 210:465
REMARK 3 ORIGIN FOR THE GROUP (A): 49.4598 44.1792 0.8624
REMARK 3 T TENSOR
REMARK 3 T11: 0.1740 T22: 0.1896
REMARK 3 T33: 0.1923 T12: 0.0185
REMARK 3 T13: -0.0019 T23: 0.0207
REMARK 3 L TENSOR
REMARK 3 L11: 0.5231 L22: 0.1181
REMARK 3 L33: 0.4289 L12: 0.0504
REMARK 3 L13: 0.1162 L23: 0.0383
REMARK 3 S TENSOR
REMARK 3 S11: -0.0195 S12: -0.0527 S13: -0.0417
REMARK 3 S21: 0.0121 S22: 0.0227 S23: 0.0113
REMARK 3 S31: -0.0268 S32: -0.0486 S33: -0.0000
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN C AND RESI 466:609
REMARK 3 ORIGIN FOR THE GROUP (A): 47.6673 63.5141 18.6823
REMARK 3 T TENSOR
REMARK 3 T11: 0.3077 T22: 0.3532
REMARK 3 T33: 0.2139 T12: 0.1136
REMARK 3 T13: -0.0021 T23: -0.0396
REMARK 3 L TENSOR
REMARK 3 L11: 0.4592 L22: 0.2993
REMARK 3 L33: 0.4763 L12: -0.1713
REMARK 3 L13: -0.1610 L23: 0.1959
REMARK 3 S TENSOR
REMARK 3 S11: -0.0422 S12: -0.2523 S13: 0.1112
REMARK 3 S21: 0.0540 S22: 0.0799 S23: -0.0369
REMARK 3 S31: -0.1954 S32: -0.1996 S33: 0.0659
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 5NI4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 23-MAR-17.
REMARK 100 THE DEPOSITION ID IS D_1200004019.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-MAR-16
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.9
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID29
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97625
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 : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 152082
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.895
REMARK 200 RESOLUTION RANGE LOW (A) : 49.810
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 6.400
REMARK 200 R MERGE (I) : 0.18850
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 6.6100
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.96
REMARK 200 COMPLETENESS FOR SHELL (%) : 99.6
REMARK 200 DATA REDUNDANCY IN SHELL : 6.30
REMARK 200 R MERGE FOR SHELL (I) : 1.60900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 0.930
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: 5NI2
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 48.57
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.39
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 8% (W/V) PEG 20 000, 15% (W/V) PEG MME
REMARK 280 550, 100 MM MES/IMIDAZOLE PH 6.9, 20 MM OF EACH ALCOHOL (1,6-
REMARK 280 HEXANEDIOL, 1-BUTANOL, (RS)-1,2-PROPANEDIOL, 2-PROPANOL, 1,4-
REMARK 280 BUTANEDIOL, 1,3-PROPANEDIOL), VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 294K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32
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
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 58.63333
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 29.31667
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3200 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 68900 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 26.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 -6
REMARK 465 HIS A -5
REMARK 465 HIS A -4
REMARK 465 HIS A -3
REMARK 465 HIS A -2
REMARK 465 HIS A -1
REMARK 465 HIS A 0
REMARK 465 PRO A 1
REMARK 465 GLU A 2
REMARK 465 ASP A 610
REMARK 465 MET B -6
REMARK 465 HIS B -5
REMARK 465 HIS B -4
REMARK 465 HIS B -3
REMARK 465 HIS B -2
REMARK 465 HIS B -1
REMARK 465 HIS B 0
REMARK 465 PRO B 1
REMARK 465 ASP B 610
REMARK 465 MET C -6
REMARK 465 HIS C -5
REMARK 465 HIS C -4
REMARK 465 HIS C -3
REMARK 465 HIS C -2
REMARK 465 HIS C -1
REMARK 465 HIS C 0
REMARK 465 PRO C 1
REMARK 465 ASP C 610
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 844 O HOH B 1489 2.08
REMARK 500 O HOH A 1023 O HOH A 1335 2.08
REMARK 500 O HOH B 1177 O HOH B 1436 2.12
REMARK 500 O HOH B 907 O HOH B 1380 2.12
REMARK 500 O HOH B 1360 O HOH B 1387 2.13
REMARK 500 O HOH C 989 O HOH C 1069 2.13
REMARK 500 CAH DJ3 A 705 O HOH A 801 2.14
REMARK 500 O HOH A 813 O HOH A 1110 2.14
REMARK 500 O HOH C 884 O HOH C 1230 2.15
REMARK 500 O HOH C 1336 O HOH C 1440 2.16
REMARK 500 O HOH C 812 O HOH C 908 2.16
REMARK 500 O HOH A 1252 O HOH A 1371 2.16
REMARK 500 O HOH A 1184 O HOH A 1290 2.16
REMARK 500 O HOH A 1447 O HOH A 1467 2.16
REMARK 500 O HOH C 1089 O HOH C 1292 2.17
REMARK 500 OE1 GLU B 412 O HOH B 802 2.17
REMARK 500 CAH DJ3 A 705 O HOH A 801 2.18
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 HZ3 LYS C 518 O HOH B 813 2665 1.59
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 GLN A 79 68.20 -119.85
REMARK 500 SER A 80 -121.40 38.36
REMARK 500 ASN A 97 -5.54 83.09
REMARK 500 LYS A 126 -3.01 72.94
REMARK 500 SER A 222 -177.12 -170.23
REMARK 500 CYS A 274 -11.17 74.02
REMARK 500 LEU A 275 82.30 -153.80
REMARK 500 PHE A 432 52.07 -101.23
REMARK 500 LYS A 546 31.66 72.58
REMARK 500 LYS A 546 30.94 73.18
REMARK 500 GLN B 79 71.04 -112.62
REMARK 500 SER B 80 -117.61 38.28
REMARK 500 ASN B 97 -6.08 79.89
REMARK 500 LYS B 126 -1.37 70.38
REMARK 500 ASP B 183 103.50 -162.90
REMARK 500 CYS B 274 -8.93 77.42
REMARK 500 LEU B 275 80.47 -157.17
REMARK 500 PHE B 432 49.82 -100.74
REMARK 500 GLN C 79 62.28 -113.48
REMARK 500 SER C 80 -129.39 51.94
REMARK 500 SER C 80 -129.55 52.30
REMARK 500 ASN C 97 -7.70 83.29
REMARK 500 ASP C 183 107.81 -163.10
REMARK 500 SER C 222 -179.30 -170.39
REMARK 500 CYS C 274 -9.44 75.23
REMARK 500 LEU C 275 83.00 -156.45
REMARK 500 TRP C 301 -60.55 -109.90
REMARK 500 PHE C 432 42.41 -100.53
REMARK 500 LYS C 546 38.02 71.17
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 A1475 DISTANCE = 6.33 ANGSTROMS
REMARK 525 HOH B1518 DISTANCE = 5.88 ANGSTROMS
REMARK 525 HOH B1519 DISTANCE = 6.10 ANGSTROMS
REMARK 525 HOH B1520 DISTANCE = 6.11 ANGSTROMS
REMARK 525 HOH B1521 DISTANCE = 6.31 ANGSTROMS
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 HOH B 801
REMARK 615 HOH B 895
REMARK 615 HOH C 801
REMARK 615 HOH C 832
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 701 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 295 NE2
REMARK 620 2 HIS A 299 NE2 103.4
REMARK 620 3 GLU A 318 OE1 95.4 107.5
REMARK 620 4 GLU A 318 OE2 151.8 89.0 56.5
REMARK 620 5 DJ3 A 705 OAT 94.9 133.6 112.8 94.4
REMARK 620 6 DJ3 A 705 OAT 95.4 137.1 108.6 92.1 4.2
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 701 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS B 295 NE2
REMARK 620 2 HIS B 299 NE2 97.3
REMARK 620 3 GLU B 318 OE1 96.8 106.3
REMARK 620 4 GLU B 318 OE2 151.5 90.4 54.7
REMARK 620 5 DJ3 B 705 OAT 98.6 132.6 115.7 96.2
REMARK 620 6 DJ3 B 705 OAT 103.1 129.2 116.7 93.0 4.9
REMARK 620 7 HOH B 808 O 83.5 78.0 175.6 125.0 59.9 59.0
REMARK 620 N 1 2 3 4 5 6
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN C 701 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS C 295 NE2
REMARK 620 2 HIS C 299 NE2 99.1
REMARK 620 3 GLU C 318 OE1 95.3 105.2
REMARK 620 4 GLU C 318 OE2 150.5 88.5 55.2
REMARK 620 5 DJ3 C 703 OAT 97.4 142.1 107.0 93.6
REMARK 620 6 DJ3 C 703 OAT 97.3 140.7 108.6 94.5 1.7
REMARK 620 7 HOH C 805 O 89.6 87.6 165.3 119.3 58.6 56.9
REMARK 620 N 1 2 3 4 5 6
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 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IMD A 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IMD A 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IMD A 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DJ3 A 705
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN B 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IMD B 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IMD B 703
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IMD B 704
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DJ3 B 705
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN C 701
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue IMD C 702
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue DJ3 C 703
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4MS6 RELATED DB: PDB
REMARK 900 RELATED ID: 4DPR RELATED DB: PDB
REMARK 900 RELATED ID: 5NI2 RELATED DB: PDB
DBREF 5NI4 A 1 610 UNP P09960 LKHA4_HUMAN 2 611
DBREF 5NI4 B 1 610 UNP P09960 LKHA4_HUMAN 2 611
DBREF 5NI4 C 1 610 UNP P09960 LKHA4_HUMAN 2 611
SEQADV 5NI4 MET A -6 UNP P09960 INITIATING METHIONINE
SEQADV 5NI4 HIS A -5 UNP P09960 EXPRESSION TAG
SEQADV 5NI4 HIS A -4 UNP P09960 EXPRESSION TAG
SEQADV 5NI4 HIS A -3 UNP P09960 EXPRESSION TAG
SEQADV 5NI4 HIS A -2 UNP P09960 EXPRESSION TAG
SEQADV 5NI4 HIS A -1 UNP P09960 EXPRESSION TAG
SEQADV 5NI4 HIS A 0 UNP P09960 EXPRESSION TAG
SEQADV 5NI4 ALA A 271 UNP P09960 GLU 272 ENGINEERED MUTATION
SEQADV 5NI4 MET B -6 UNP P09960 INITIATING METHIONINE
SEQADV 5NI4 HIS B -5 UNP P09960 EXPRESSION TAG
SEQADV 5NI4 HIS B -4 UNP P09960 EXPRESSION TAG
SEQADV 5NI4 HIS B -3 UNP P09960 EXPRESSION TAG
SEQADV 5NI4 HIS B -2 UNP P09960 EXPRESSION TAG
SEQADV 5NI4 HIS B -1 UNP P09960 EXPRESSION TAG
SEQADV 5NI4 HIS B 0 UNP P09960 EXPRESSION TAG
SEQADV 5NI4 ALA B 271 UNP P09960 GLU 272 ENGINEERED MUTATION
SEQADV 5NI4 MET C -6 UNP P09960 INITIATING METHIONINE
SEQADV 5NI4 HIS C -5 UNP P09960 EXPRESSION TAG
SEQADV 5NI4 HIS C -4 UNP P09960 EXPRESSION TAG
SEQADV 5NI4 HIS C -3 UNP P09960 EXPRESSION TAG
SEQADV 5NI4 HIS C -2 UNP P09960 EXPRESSION TAG
SEQADV 5NI4 HIS C -1 UNP P09960 EXPRESSION TAG
SEQADV 5NI4 HIS C 0 UNP P09960 EXPRESSION TAG
SEQADV 5NI4 ALA C 271 UNP P09960 GLU 272 ENGINEERED MUTATION
SEQRES 1 A 617 MET HIS HIS HIS HIS HIS HIS PRO GLU ILE VAL ASP THR
SEQRES 2 A 617 CYS SER LEU ALA SER PRO ALA SER VAL CYS ARG THR LYS
SEQRES 3 A 617 HIS LEU HIS LEU ARG CYS SER VAL ASP PHE THR ARG ARG
SEQRES 4 A 617 THR LEU THR GLY THR ALA ALA LEU THR VAL GLN SER GLN
SEQRES 5 A 617 GLU ASP ASN LEU ARG SER LEU VAL LEU ASP THR LYS ASP
SEQRES 6 A 617 LEU THR ILE GLU LYS VAL VAL ILE ASN GLY GLN GLU VAL
SEQRES 7 A 617 LYS TYR ALA LEU GLY GLU ARG GLN SER TYR LYS GLY SER
SEQRES 8 A 617 PRO MET GLU ILE SER LEU PRO ILE ALA LEU SER LYS ASN
SEQRES 9 A 617 GLN GLU ILE VAL ILE GLU ILE SER PHE GLU THR SER PRO
SEQRES 10 A 617 LYS SER SER ALA LEU GLN TRP LEU THR PRO GLU GLN THR
SEQRES 11 A 617 SER GLY LYS GLU HIS PRO TYR LEU PHE SER GLN CYS GLN
SEQRES 12 A 617 ALA ILE HIS CYS ARG ALA ILE LEU PRO CYS GLN ASP THR
SEQRES 13 A 617 PRO SER VAL LYS LEU THR TYR THR ALA GLU VAL SER VAL
SEQRES 14 A 617 PRO LYS GLU LEU VAL ALA LEU MET SER ALA ILE ARG ASP
SEQRES 15 A 617 GLY GLU THR PRO ASP PRO GLU ASP PRO SER ARG LYS ILE
SEQRES 16 A 617 TYR LYS PHE ILE GLN LYS VAL PRO ILE PRO CYS TYR LEU
SEQRES 17 A 617 ILE ALA LEU VAL VAL GLY ALA LEU GLU SER ARG GLN ILE
SEQRES 18 A 617 GLY PRO ARG THR LEU VAL TRP SER GLU LYS GLU GLN VAL
SEQRES 19 A 617 GLU LYS SER ALA TYR GLU PHE SER GLU THR GLU SER MET
SEQRES 20 A 617 LEU LYS ILE ALA GLU ASP LEU GLY GLY PRO TYR VAL TRP
SEQRES 21 A 617 GLY GLN TYR ASP LEU LEU VAL LEU PRO PRO SER PHE PRO
SEQRES 22 A 617 TYR GLY GLY MET ALA ASN PRO CYS LEU THR PHE VAL THR
SEQRES 23 A 617 PRO THR LEU LEU ALA GLY ASP LYS SER LEU SER ASN VAL
SEQRES 24 A 617 ILE ALA HIS GLU ILE SER HIS SER TRP THR GLY ASN LEU
SEQRES 25 A 617 VAL THR ASN LYS THR TRP ASP HIS PHE TRP LEU ASN GLU
SEQRES 26 A 617 GLY HIS THR VAL TYR LEU GLU ARG HIS ILE CYS GLY ARG
SEQRES 27 A 617 LEU PHE GLY GLU LYS PHE ARG HIS PHE ASN ALA LEU GLY
SEQRES 28 A 617 GLY TRP GLY GLU LEU GLN ASN SER VAL LYS THR PHE GLY
SEQRES 29 A 617 GLU THR HIS PRO PHE THR LYS LEU VAL VAL ASP LEU THR
SEQRES 30 A 617 ASP ILE ASP PRO ASP VAL ALA TYR SER SER VAL PRO TYR
SEQRES 31 A 617 GLU LYS GLY PHE ALA LEU LEU PHE TYR LEU GLU GLN LEU
SEQRES 32 A 617 LEU GLY GLY PRO GLU ILE PHE LEU GLY PHE LEU LYS ALA
SEQRES 33 A 617 TYR VAL GLU LYS PHE SER TYR LYS SER ILE THR THR ASP
SEQRES 34 A 617 ASP TRP LYS ASP PHE LEU TYR SER TYR PHE LYS ASP LYS
SEQRES 35 A 617 VAL ASP VAL LEU ASN GLN VAL ASP TRP ASN ALA TRP LEU
SEQRES 36 A 617 TYR SER PRO GLY LEU PRO PRO ILE LYS PRO ASN TYR ASP
SEQRES 37 A 617 MET THR LEU THR ASN ALA CYS ILE ALA LEU SER GLN ARG
SEQRES 38 A 617 TRP ILE THR ALA LYS GLU ASP ASP LEU ASN SER PHE ASN
SEQRES 39 A 617 ALA THR ASP LEU LYS ASP LEU SER SER HIS GLN LEU ASN
SEQRES 40 A 617 GLU PHE LEU ALA GLN THR LEU GLN ARG ALA PRO LEU PRO
SEQRES 41 A 617 LEU GLY HIS ILE LYS ARG MET GLN GLU VAL TYR ASN PHE
SEQRES 42 A 617 ASN ALA ILE ASN ASN SER GLU ILE ARG PHE ARG TRP LEU
SEQRES 43 A 617 ARG LEU CYS ILE GLN SER LYS TRP GLU ASP ALA ILE PRO
SEQRES 44 A 617 LEU ALA LEU LYS MET ALA THR GLU GLN GLY ARG MET LYS
SEQRES 45 A 617 PHE THR ARG PRO LEU PHE LYS ASP LEU ALA ALA PHE ASP
SEQRES 46 A 617 LYS SER HIS ASP GLN ALA VAL ARG THR TYR GLN GLU HIS
SEQRES 47 A 617 LYS ALA SER MET HIS PRO VAL THR ALA MET LEU VAL GLY
SEQRES 48 A 617 LYS ASP LEU LYS VAL ASP
SEQRES 1 B 617 MET HIS HIS HIS HIS HIS HIS PRO GLU ILE VAL ASP THR
SEQRES 2 B 617 CYS SER LEU ALA SER PRO ALA SER VAL CYS ARG THR LYS
SEQRES 3 B 617 HIS LEU HIS LEU ARG CYS SER VAL ASP PHE THR ARG ARG
SEQRES 4 B 617 THR LEU THR GLY THR ALA ALA LEU THR VAL GLN SER GLN
SEQRES 5 B 617 GLU ASP ASN LEU ARG SER LEU VAL LEU ASP THR LYS ASP
SEQRES 6 B 617 LEU THR ILE GLU LYS VAL VAL ILE ASN GLY GLN GLU VAL
SEQRES 7 B 617 LYS TYR ALA LEU GLY GLU ARG GLN SER TYR LYS GLY SER
SEQRES 8 B 617 PRO MET GLU ILE SER LEU PRO ILE ALA LEU SER LYS ASN
SEQRES 9 B 617 GLN GLU ILE VAL ILE GLU ILE SER PHE GLU THR SER PRO
SEQRES 10 B 617 LYS SER SER ALA LEU GLN TRP LEU THR PRO GLU GLN THR
SEQRES 11 B 617 SER GLY LYS GLU HIS PRO TYR LEU PHE SER GLN CYS GLN
SEQRES 12 B 617 ALA ILE HIS CYS ARG ALA ILE LEU PRO CYS GLN ASP THR
SEQRES 13 B 617 PRO SER VAL LYS LEU THR TYR THR ALA GLU VAL SER VAL
SEQRES 14 B 617 PRO LYS GLU LEU VAL ALA LEU MET SER ALA ILE ARG ASP
SEQRES 15 B 617 GLY GLU THR PRO ASP PRO GLU ASP PRO SER ARG LYS ILE
SEQRES 16 B 617 TYR LYS PHE ILE GLN LYS VAL PRO ILE PRO CYS TYR LEU
SEQRES 17 B 617 ILE ALA LEU VAL VAL GLY ALA LEU GLU SER ARG GLN ILE
SEQRES 18 B 617 GLY PRO ARG THR LEU VAL TRP SER GLU LYS GLU GLN VAL
SEQRES 19 B 617 GLU LYS SER ALA TYR GLU PHE SER GLU THR GLU SER MET
SEQRES 20 B 617 LEU LYS ILE ALA GLU ASP LEU GLY GLY PRO TYR VAL TRP
SEQRES 21 B 617 GLY GLN TYR ASP LEU LEU VAL LEU PRO PRO SER PHE PRO
SEQRES 22 B 617 TYR GLY GLY MET ALA ASN PRO CYS LEU THR PHE VAL THR
SEQRES 23 B 617 PRO THR LEU LEU ALA GLY ASP LYS SER LEU SER ASN VAL
SEQRES 24 B 617 ILE ALA HIS GLU ILE SER HIS SER TRP THR GLY ASN LEU
SEQRES 25 B 617 VAL THR ASN LYS THR TRP ASP HIS PHE TRP LEU ASN GLU
SEQRES 26 B 617 GLY HIS THR VAL TYR LEU GLU ARG HIS ILE CYS GLY ARG
SEQRES 27 B 617 LEU PHE GLY GLU LYS PHE ARG HIS PHE ASN ALA LEU GLY
SEQRES 28 B 617 GLY TRP GLY GLU LEU GLN ASN SER VAL LYS THR PHE GLY
SEQRES 29 B 617 GLU THR HIS PRO PHE THR LYS LEU VAL VAL ASP LEU THR
SEQRES 30 B 617 ASP ILE ASP PRO ASP VAL ALA TYR SER SER VAL PRO TYR
SEQRES 31 B 617 GLU LYS GLY PHE ALA LEU LEU PHE TYR LEU GLU GLN LEU
SEQRES 32 B 617 LEU GLY GLY PRO GLU ILE PHE LEU GLY PHE LEU LYS ALA
SEQRES 33 B 617 TYR VAL GLU LYS PHE SER TYR LYS SER ILE THR THR ASP
SEQRES 34 B 617 ASP TRP LYS ASP PHE LEU TYR SER TYR PHE LYS ASP LYS
SEQRES 35 B 617 VAL ASP VAL LEU ASN GLN VAL ASP TRP ASN ALA TRP LEU
SEQRES 36 B 617 TYR SER PRO GLY LEU PRO PRO ILE LYS PRO ASN TYR ASP
SEQRES 37 B 617 MET THR LEU THR ASN ALA CYS ILE ALA LEU SER GLN ARG
SEQRES 38 B 617 TRP ILE THR ALA LYS GLU ASP ASP LEU ASN SER PHE ASN
SEQRES 39 B 617 ALA THR ASP LEU LYS ASP LEU SER SER HIS GLN LEU ASN
SEQRES 40 B 617 GLU PHE LEU ALA GLN THR LEU GLN ARG ALA PRO LEU PRO
SEQRES 41 B 617 LEU GLY HIS ILE LYS ARG MET GLN GLU VAL TYR ASN PHE
SEQRES 42 B 617 ASN ALA ILE ASN ASN SER GLU ILE ARG PHE ARG TRP LEU
SEQRES 43 B 617 ARG LEU CYS ILE GLN SER LYS TRP GLU ASP ALA ILE PRO
SEQRES 44 B 617 LEU ALA LEU LYS MET ALA THR GLU GLN GLY ARG MET LYS
SEQRES 45 B 617 PHE THR ARG PRO LEU PHE LYS ASP LEU ALA ALA PHE ASP
SEQRES 46 B 617 LYS SER HIS ASP GLN ALA VAL ARG THR TYR GLN GLU HIS
SEQRES 47 B 617 LYS ALA SER MET HIS PRO VAL THR ALA MET LEU VAL GLY
SEQRES 48 B 617 LYS ASP LEU LYS VAL ASP
SEQRES 1 C 617 MET HIS HIS HIS HIS HIS HIS PRO GLU ILE VAL ASP THR
SEQRES 2 C 617 CYS SER LEU ALA SER PRO ALA SER VAL CYS ARG THR LYS
SEQRES 3 C 617 HIS LEU HIS LEU ARG CYS SER VAL ASP PHE THR ARG ARG
SEQRES 4 C 617 THR LEU THR GLY THR ALA ALA LEU THR VAL GLN SER GLN
SEQRES 5 C 617 GLU ASP ASN LEU ARG SER LEU VAL LEU ASP THR LYS ASP
SEQRES 6 C 617 LEU THR ILE GLU LYS VAL VAL ILE ASN GLY GLN GLU VAL
SEQRES 7 C 617 LYS TYR ALA LEU GLY GLU ARG GLN SER TYR LYS GLY SER
SEQRES 8 C 617 PRO MET GLU ILE SER LEU PRO ILE ALA LEU SER LYS ASN
SEQRES 9 C 617 GLN GLU ILE VAL ILE GLU ILE SER PHE GLU THR SER PRO
SEQRES 10 C 617 LYS SER SER ALA LEU GLN TRP LEU THR PRO GLU GLN THR
SEQRES 11 C 617 SER GLY LYS GLU HIS PRO TYR LEU PHE SER GLN CYS GLN
SEQRES 12 C 617 ALA ILE HIS CYS ARG ALA ILE LEU PRO CYS GLN ASP THR
SEQRES 13 C 617 PRO SER VAL LYS LEU THR TYR THR ALA GLU VAL SER VAL
SEQRES 14 C 617 PRO LYS GLU LEU VAL ALA LEU MET SER ALA ILE ARG ASP
SEQRES 15 C 617 GLY GLU THR PRO ASP PRO GLU ASP PRO SER ARG LYS ILE
SEQRES 16 C 617 TYR LYS PHE ILE GLN LYS VAL PRO ILE PRO CYS TYR LEU
SEQRES 17 C 617 ILE ALA LEU VAL VAL GLY ALA LEU GLU SER ARG GLN ILE
SEQRES 18 C 617 GLY PRO ARG THR LEU VAL TRP SER GLU LYS GLU GLN VAL
SEQRES 19 C 617 GLU LYS SER ALA TYR GLU PHE SER GLU THR GLU SER MET
SEQRES 20 C 617 LEU LYS ILE ALA GLU ASP LEU GLY GLY PRO TYR VAL TRP
SEQRES 21 C 617 GLY GLN TYR ASP LEU LEU VAL LEU PRO PRO SER PHE PRO
SEQRES 22 C 617 TYR GLY GLY MET ALA ASN PRO CYS LEU THR PHE VAL THR
SEQRES 23 C 617 PRO THR LEU LEU ALA GLY ASP LYS SER LEU SER ASN VAL
SEQRES 24 C 617 ILE ALA HIS GLU ILE SER HIS SER TRP THR GLY ASN LEU
SEQRES 25 C 617 VAL THR ASN LYS THR TRP ASP HIS PHE TRP LEU ASN GLU
SEQRES 26 C 617 GLY HIS THR VAL TYR LEU GLU ARG HIS ILE CYS GLY ARG
SEQRES 27 C 617 LEU PHE GLY GLU LYS PHE ARG HIS PHE ASN ALA LEU GLY
SEQRES 28 C 617 GLY TRP GLY GLU LEU GLN ASN SER VAL LYS THR PHE GLY
SEQRES 29 C 617 GLU THR HIS PRO PHE THR LYS LEU VAL VAL ASP LEU THR
SEQRES 30 C 617 ASP ILE ASP PRO ASP VAL ALA TYR SER SER VAL PRO TYR
SEQRES 31 C 617 GLU LYS GLY PHE ALA LEU LEU PHE TYR LEU GLU GLN LEU
SEQRES 32 C 617 LEU GLY GLY PRO GLU ILE PHE LEU GLY PHE LEU LYS ALA
SEQRES 33 C 617 TYR VAL GLU LYS PHE SER TYR LYS SER ILE THR THR ASP
SEQRES 34 C 617 ASP TRP LYS ASP PHE LEU TYR SER TYR PHE LYS ASP LYS
SEQRES 35 C 617 VAL ASP VAL LEU ASN GLN VAL ASP TRP ASN ALA TRP LEU
SEQRES 36 C 617 TYR SER PRO GLY LEU PRO PRO ILE LYS PRO ASN TYR ASP
SEQRES 37 C 617 MET THR LEU THR ASN ALA CYS ILE ALA LEU SER GLN ARG
SEQRES 38 C 617 TRP ILE THR ALA LYS GLU ASP ASP LEU ASN SER PHE ASN
SEQRES 39 C 617 ALA THR ASP LEU LYS ASP LEU SER SER HIS GLN LEU ASN
SEQRES 40 C 617 GLU PHE LEU ALA GLN THR LEU GLN ARG ALA PRO LEU PRO
SEQRES 41 C 617 LEU GLY HIS ILE LYS ARG MET GLN GLU VAL TYR ASN PHE
SEQRES 42 C 617 ASN ALA ILE ASN ASN SER GLU ILE ARG PHE ARG TRP LEU
SEQRES 43 C 617 ARG LEU CYS ILE GLN SER LYS TRP GLU ASP ALA ILE PRO
SEQRES 44 C 617 LEU ALA LEU LYS MET ALA THR GLU GLN GLY ARG MET LYS
SEQRES 45 C 617 PHE THR ARG PRO LEU PHE LYS ASP LEU ALA ALA PHE ASP
SEQRES 46 C 617 LYS SER HIS ASP GLN ALA VAL ARG THR TYR GLN GLU HIS
SEQRES 47 C 617 LYS ALA SER MET HIS PRO VAL THR ALA MET LEU VAL GLY
SEQRES 48 C 617 LYS ASP LEU LYS VAL ASP
HET ZN A 701 1
HET IMD A 702 10
HET IMD A 703 10
HET IMD A 704 10
HET DJ3 A 705 104
HET ZN B 701 1
HET IMD B 702 10
HET IMD B 703 10
HET IMD B 704 10
HET DJ3 B 705 104
HET ZN C 701 1
HET IMD C 702 10
HET DJ3 C 703 104
HETNAM ZN ZINC ION
HETNAM IMD IMIDAZOLE
HETNAM DJ3 5S-5,6-OXIDO-7,9-TRANS-11,14-CIS-EICOSATETRAENOIC ACID
FORMUL 4 ZN 3(ZN 2+)
FORMUL 5 IMD 7(C3 H5 N2 1+)
FORMUL 8 DJ3 3(C20 H30 O3)
FORMUL 17 HOH *2056(H2 O)
HELIX 1 AA1 GLN A 79 GLY A 83 5 5
HELIX 2 AA2 THR A 119 THR A 123 5 5
HELIX 3 AA3 HIS A 139 ILE A 143 5 5
HELIX 4 AA4 PRO A 198 ILE A 202 5 5
HELIX 5 AA5 GLU A 223 PHE A 234 1 12
HELIX 6 AA6 GLU A 236 GLY A 249 1 14
HELIX 7 AA7 PRO A 280 LEU A 283 5 4
HELIX 8 AA8 SER A 290 HIS A 299 1 10
HELIX 9 AA9 THR A 310 ASP A 312 5 3
HELIX 10 AB1 HIS A 313 GLY A 334 1 22
HELIX 11 AB2 GLY A 334 GLY A 357 1 24
HELIX 12 AB3 HIS A 360 LYS A 364 5 5
HELIX 13 AB4 ASP A 373 TYR A 378 1 6
HELIX 14 AB5 SER A 380 GLY A 398 1 19
HELIX 15 AB6 GLY A 399 SER A 415 1 17
HELIX 16 AB7 THR A 420 PHE A 432 1 13
HELIX 17 AB8 LYS A 435 ASN A 440 1 6
HELIX 18 AB9 ASP A 443 SER A 450 1 8
HELIX 19 AC1 THR A 465 THR A 477 1 13
HELIX 20 AC2 LYS A 479 PHE A 486 5 8
HELIX 21 AC3 ASN A 487 LYS A 492 5 6
HELIX 22 AC4 SER A 495 ARG A 509 1 15
HELIX 23 AC5 PRO A 513 ASN A 525 1 13
HELIX 24 AC6 PHE A 526 ILE A 529 5 4
HELIX 25 AC7 ASN A 531 SER A 545 1 15
HELIX 26 AC8 TRP A 547 ASP A 549 5 3
HELIX 27 AC9 ALA A 550 GLN A 561 1 12
HELIX 28 AD1 ARG A 563 PHE A 577 1 15
HELIX 29 AD2 SER A 580 LYS A 592 1 13
HELIX 30 AD3 ALA A 593 MET A 595 5 3
HELIX 31 AD4 HIS A 596 LEU A 607 1 12
HELIX 32 AD5 GLN B 79 GLY B 83 5 5
HELIX 33 AD6 THR B 119 THR B 123 5 5
HELIX 34 AD7 HIS B 139 ILE B 143 5 5
HELIX 35 AD8 PRO B 198 ILE B 202 5 5
HELIX 36 AD9 GLU B 223 PHE B 234 1 12
HELIX 37 AE1 GLU B 236 GLY B 249 1 14
HELIX 38 AE2 PRO B 280 LEU B 283 5 4
HELIX 39 AE3 SER B 290 HIS B 299 1 10
HELIX 40 AE4 THR B 310 ASP B 312 5 3
HELIX 41 AE5 HIS B 313 GLY B 334 1 22
HELIX 42 AE6 GLY B 334 GLY B 357 1 24
HELIX 43 AE7 HIS B 360 LYS B 364 5 5
HELIX 44 AE8 ASP B 373 TYR B 378 1 6
HELIX 45 AE9 SER B 380 GLY B 398 1 19
HELIX 46 AF1 GLY B 399 SER B 415 1 17
HELIX 47 AF2 THR B 420 PHE B 432 1 13
HELIX 48 AF3 LYS B 435 ASN B 440 1 6
HELIX 49 AF4 ASP B 443 SER B 450 1 8
HELIX 50 AF5 THR B 465 THR B 477 1 13
HELIX 51 AF6 LYS B 479 PHE B 486 5 8
HELIX 52 AF7 ASN B 487 LYS B 492 5 6
HELIX 53 AF8 SER B 495 GLN B 508 1 14
HELIX 54 AF9 PRO B 513 ASN B 525 1 13
HELIX 55 AG1 PHE B 526 ILE B 529 5 4
HELIX 56 AG2 ASN B 531 SER B 545 1 15
HELIX 57 AG3 TRP B 547 ASP B 549 5 3
HELIX 58 AG4 ALA B 550 GLN B 561 1 12
HELIX 59 AG5 ARG B 563 PHE B 577 1 15
HELIX 60 AG6 SER B 580 LYS B 592 1 13
HELIX 61 AG7 ALA B 593 MET B 595 5 3
HELIX 62 AG8 HIS B 596 LYS B 608 1 13
HELIX 63 AG9 GLN C 79 GLY C 83 5 5
HELIX 64 AH1 THR C 119 THR C 123 5 5
HELIX 65 AH2 HIS C 139 ILE C 143 5 5
HELIX 66 AH3 PRO C 198 ILE C 202 5 5
HELIX 67 AH4 GLN C 226 PHE C 234 1 9
HELIX 68 AH5 GLU C 236 GLY C 249 1 14
HELIX 69 AH6 PRO C 280 LEU C 283 5 4
HELIX 70 AH7 SER C 290 HIS C 299 1 10
HELIX 71 AH8 THR C 310 ASP C 312 5 3
HELIX 72 AH9 HIS C 313 GLY C 334 1 22
HELIX 73 AI1 GLY C 334 GLY C 357 1 24
HELIX 74 AI2 HIS C 360 LYS C 364 5 5
HELIX 75 AI3 ASP C 373 TYR C 378 1 6
HELIX 76 AI4 SER C 380 GLY C 398 1 19
HELIX 77 AI5 GLY C 399 SER C 415 1 17
HELIX 78 AI6 THR C 420 PHE C 432 1 13
HELIX 79 AI7 LYS C 435 ASN C 440 1 6
HELIX 80 AI8 ASP C 443 SER C 450 1 8
HELIX 81 AI9 THR C 465 ALA C 478 1 14
HELIX 82 AJ1 LYS C 479 PHE C 486 5 8
HELIX 83 AJ2 ASN C 487 LYS C 492 5 6
HELIX 84 AJ3 SER C 495 GLN C 508 1 14
HELIX 85 AJ4 PRO C 513 ASN C 525 1 13
HELIX 86 AJ5 PHE C 526 ILE C 529 5 4
HELIX 87 AJ6 ASN C 531 SER C 545 1 15
HELIX 88 AJ7 TRP C 547 ASP C 549 5 3
HELIX 89 AJ8 ALA C 550 GLN C 561 1 12
HELIX 90 AJ9 ARG C 563 PHE C 577 1 15
HELIX 91 AK1 SER C 580 LYS C 592 1 13
HELIX 92 AK2 ALA C 593 MET C 595 5 3
HELIX 93 AK3 HIS C 596 LYS C 608 1 13
SHEET 1 AA1 8 GLN A 69 GLU A 70 0
SHEET 2 AA1 8 LEU A 59 ILE A 66 -1 N ILE A 66 O GLN A 69
SHEET 3 AA1 8 GLU A 99 THR A 108 -1 O GLU A 103 N VAL A 65
SHEET 4 AA1 8 THR A 33 SER A 44 -1 N VAL A 42 O ILE A 100
SHEET 5 AA1 8 CYS A 16 ASP A 28 -1 N LYS A 19 O THR A 41
SHEET 6 AA1 8 LEU A 154 PRO A 163 1 O THR A 157 N LEU A 23
SHEET 7 AA1 8 ARG A 186 ILE A 197 -1 O GLN A 193 N TYR A 156
SHEET 8 AA1 8 ILE A 173 PRO A 179 -1 N THR A 178 O ILE A 188
SHEET 1 AA2 3 LEU A 49 THR A 56 0
SHEET 2 AA2 3 SER A 84 LEU A 94 -1 O ILE A 88 N LEU A 52
SHEET 3 AA2 3 TYR A 73 LEU A 75 -1 N ALA A 74 O GLU A 87
SHEET 1 AA3 4 LEU A 115 LEU A 118 0
SHEET 2 AA3 4 TYR A 130 SER A 133 -1 O TYR A 130 N LEU A 118
SHEET 3 AA3 4 LEU A 204 GLY A 207 -1 O VAL A 206 N LEU A 131
SHEET 4 AA3 4 VAL A 167 MET A 170 -1 N VAL A 167 O GLY A 207
SHEET 1 AA4 5 GLU A 210 GLY A 215 0
SHEET 2 AA4 5 THR A 218 SER A 222 -1 O SER A 222 N GLU A 210
SHEET 3 AA4 5 ASP A 257 VAL A 260 1 O LEU A 258 N TRP A 221
SHEET 4 AA4 5 LEU A 275 VAL A 278 1 O THR A 276 N LEU A 259
SHEET 5 AA4 5 GLY A 269 MET A 270 -1 N MET A 270 O PHE A 277
SHEET 1 AA5 2 VAL A 306 ASN A 308 0
SHEET 2 AA5 2 LYS A 417 ILE A 419 1 O ILE A 419 N THR A 307
SHEET 1 AA6 8 GLN B 69 GLU B 70 0
SHEET 2 AA6 8 THR B 60 ILE B 66 -1 N ILE B 66 O GLN B 69
SHEET 3 AA6 8 GLU B 99 GLU B 107 -1 O GLU B 103 N VAL B 65
SHEET 4 AA6 8 THR B 33 SER B 44 -1 N LEU B 40 O ILE B 102
SHEET 5 AA6 8 CYS B 16 ASP B 28 -1 N LYS B 19 O THR B 41
SHEET 6 AA6 8 LEU B 154 PRO B 163 1 O SER B 161 N VAL B 27
SHEET 7 AA6 8 ARG B 186 ILE B 197 -1 O LYS B 187 N VAL B 162
SHEET 8 AA6 8 ILE B 173 PRO B 179 -1 N THR B 178 O ILE B 188
SHEET 1 AA7 3 LEU B 49 LEU B 54 0
SHEET 2 AA7 3 MET B 86 LEU B 94 -1 O ILE B 88 N LEU B 52
SHEET 3 AA7 3 TYR B 73 LEU B 75 -1 N ALA B 74 O GLU B 87
SHEET 1 AA8 4 LEU B 115 LEU B 118 0
SHEET 2 AA8 4 TYR B 130 SER B 133 -1 O TYR B 130 N LEU B 118
SHEET 3 AA8 4 LEU B 204 GLY B 207 -1 O VAL B 206 N LEU B 131
SHEET 4 AA8 4 VAL B 167 MET B 170 -1 N VAL B 167 O GLY B 207
SHEET 1 AA9 5 GLU B 210 GLY B 215 0
SHEET 2 AA9 5 THR B 218 SER B 222 -1 O SER B 222 N GLU B 210
SHEET 3 AA9 5 ASP B 257 VAL B 260 1 O LEU B 258 N TRP B 221
SHEET 4 AA9 5 LEU B 275 VAL B 278 1 O THR B 276 N LEU B 259
SHEET 5 AA9 5 GLY B 269 MET B 270 -1 N MET B 270 O PHE B 277
SHEET 1 AB1 2 THR B 307 ASN B 308 0
SHEET 2 AB1 2 SER B 418 ILE B 419 1 O ILE B 419 N THR B 307
SHEET 1 AB2 8 GLN C 69 GLU C 70 0
SHEET 2 AB2 8 LEU C 59 ILE C 66 -1 N ILE C 66 O GLN C 69
SHEET 3 AB2 8 GLU C 99 THR C 108 -1 O GLU C 103 N VAL C 65
SHEET 4 AB2 8 THR C 33 SER C 44 -1 N LEU C 40 O ILE C 102
SHEET 5 AB2 8 CYS C 16 ASP C 28 -1 N LYS C 19 O THR C 41
SHEET 6 AB2 8 LEU C 154 PRO C 163 1 O SER C 161 N VAL C 27
SHEET 7 AB2 8 ARG C 186 ILE C 197 -1 O GLN C 193 N TYR C 156
SHEET 8 AB2 8 ILE C 173 PRO C 179 -1 N THR C 178 O ILE C 188
SHEET 1 AB3 3 LEU C 49 LEU C 54 0
SHEET 2 AB3 3 MET C 86 LEU C 94 -1 O ILE C 88 N LEU C 52
SHEET 3 AB3 3 TYR C 73 LEU C 75 -1 N ALA C 74 O GLU C 87
SHEET 1 AB4 4 LEU C 115 LEU C 118 0
SHEET 2 AB4 4 TYR C 130 SER C 133 -1 O TYR C 130 N LEU C 118
SHEET 3 AB4 4 LEU C 204 GLY C 207 -1 O VAL C 206 N LEU C 131
SHEET 4 AB4 4 VAL C 167 MET C 170 -1 N VAL C 167 O GLY C 207
SHEET 1 AB5 5 GLU C 210 GLY C 215 0
SHEET 2 AB5 5 THR C 218 SER C 222 -1 O SER C 222 N GLU C 210
SHEET 3 AB5 5 ASP C 257 VAL C 260 1 O LEU C 258 N TRP C 221
SHEET 4 AB5 5 LEU C 275 VAL C 278 1 O VAL C 278 N LEU C 259
SHEET 5 AB5 5 GLY C 269 MET C 270 -1 N MET C 270 O PHE C 277
SHEET 1 AB6 2 VAL C 306 ASN C 308 0
SHEET 2 AB6 2 LYS C 417 ILE C 419 1 O ILE C 419 N THR C 307
LINK NE2 HIS A 295 ZN ZN A 701 1555 1555 2.15
LINK NE2 HIS A 299 ZN ZN A 701 1555 1555 2.12
LINK OE1 GLU A 318 ZN ZN A 701 1555 1555 2.03
LINK OE2 GLU A 318 ZN ZN A 701 1555 1555 2.52
LINK ZN ZN A 701 OATADJ3 A 705 1555 1555 2.07
LINK ZN ZN A 701 OATBDJ3 A 705 1555 1555 2.44
LINK NE2 HIS B 295 ZN ZN B 701 1555 1555 2.09
LINK NE2 HIS B 299 ZN ZN B 701 1555 1555 2.03
LINK OE1 GLU B 318 ZN ZN B 701 1555 1555 2.01
LINK OE2 GLU B 318 ZN ZN B 701 1555 1555 2.60
LINK ZN ZN B 701 OATADJ3 B 705 1555 1555 2.01
LINK ZN ZN B 701 OATBDJ3 B 705 1555 1555 1.85
LINK ZN ZN B 701 O HOH B 808 1555 1555 2.65
LINK NE2 HIS C 295 ZN ZN C 701 1555 1555 2.11
LINK NE2 HIS C 299 ZN ZN C 701 1555 1555 2.08
LINK OE1 GLU C 318 ZN ZN C 701 1555 1555 1.98
LINK OE2 GLU C 318 ZN ZN C 701 1555 1555 2.59
LINK ZN ZN C 701 OATADJ3 C 703 1555 1555 2.02
LINK ZN ZN C 701 OATBDJ3 C 703 1555 1555 2.04
LINK ZN ZN C 701 O HOH C 805 1555 1555 2.65
CISPEP 1 GLN A 136 ALA A 137 0 4.18
CISPEP 2 ALA A 510 PRO A 511 0 2.64
CISPEP 3 GLN B 136 ALA B 137 0 4.43
CISPEP 4 ALA B 510 PRO B 511 0 1.44
CISPEP 5 GLN C 136 ALA C 137 0 4.10
CISPEP 6 ALA C 510 PRO C 511 0 1.71
SITE 1 AC1 5 HIS A 295 HIS A 299 GLU A 318 DJ3 A 705
SITE 2 AC1 5 HOH A 804
SITE 1 AC2 6 GLY A 344 GLY A 347 GLU A 348 GLU A 501
SITE 2 AC2 6 GLN A 508 HOH A1206
SITE 1 AC3 7 GLY A 248 PRO A 250 VAL A 252 GLU A 412
SITE 2 AC3 7 SER A 415 HOH A1002 HOH A1152
SITE 1 AC4 4 ASP A 422 ASP A 426 HOH A1004 HOH A1385
SITE 1 AC5 20 GLN A 136 ALA A 137 TYR A 267 GLY A 268
SITE 2 AC5 20 GLY A 269 MET A 270 HIS A 295 GLU A 296
SITE 3 AC5 20 TRP A 311 PHE A 314 GLU A 318 VAL A 367
SITE 4 AC5 20 TYR A 378 TYR A 383 ARG A 563 ZN A 701
SITE 5 AC5 20 HOH A 801 HOH A 804 HOH A 810 HOH A1145
SITE 1 AC6 5 HIS B 295 HIS B 299 GLU B 318 DJ3 B 705
SITE 2 AC6 5 HOH B 808
SITE 1 AC7 6 GLY B 344 GLY B 347 GLU B 348 GLU B 501
SITE 2 AC7 6 ALA B 504 GLN B 508
SITE 1 AC8 2 ASP B 422 ASP B 426
SITE 1 AC9 10 GLY B 248 GLY B 249 PRO B 250 LEU B 305
SITE 2 AC9 10 VAL B 411 GLU B 412 SER B 415 HOH B 896
SITE 3 AC9 10 HOH B 988 HOH B1063
SITE 1 AD1 21 GLN B 136 ALA B 137 TYR B 267 GLY B 268
SITE 2 AD1 21 GLY B 269 HIS B 295 GLU B 296 HIS B 299
SITE 3 AD1 21 TRP B 311 PHE B 314 GLU B 318 VAL B 367
SITE 4 AD1 21 PRO B 374 TYR B 378 TYR B 383 ARG B 563
SITE 5 AD1 21 LYS B 565 ZN B 701 HOH B 808 HOH B 870
SITE 6 AD1 21 HOH B1007
SITE 1 AD2 5 HIS C 295 HIS C 299 GLU C 318 DJ3 C 703
SITE 2 AD2 5 HOH C 805
SITE 1 AD3 7 GLY C 344 GLY C 347 GLU C 348 ASN C 351
SITE 2 AD3 7 GLU C 501 ALA C 504 GLN C 508
SITE 1 AD4 22 GLN C 136 ALA C 137 TYR C 267 GLY C 268
SITE 2 AD4 22 GLY C 269 MET C 270 HIS C 295 GLU C 296
SITE 3 AD4 22 TRP C 311 PHE C 314 GLU C 318 VAL C 367
SITE 4 AD4 22 PRO C 374 TYR C 383 ARG C 563 LYS C 565
SITE 5 AD4 22 ZN C 701 HOH C 805 HOH C 865 HOH C1025
SITE 6 AD4 22 HOH C1169 HOH C1203
CRYST1 139.560 139.560 87.950 90.00 90.00 120.00 P 32 9
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 0.007165 0.004137 0.000000 0.00000
SCALE2 0.000000 0.008274 0.000000 0.00000
SCALE3 0.000000 0.000000 0.011370 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
