HEADER TRANSFERASE 30-JUN-15 5CB8
TITLE CRYSTAL STRUCTURE OF ADENOSINE-5'-PHOSPHOSULFATE KINASE IN COMPLEX
TITLE 2 WITH APS AND SULFATE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROBABLE ADENYLYL-SULFATE KINASE;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: APS KINASE,ATP ADENOSINE-5'-PHOSPHOSULFATE 3'-
COMPND 5 PHOSPHOTRANSFERASE,ADENOSINE-5'-PHOSPHOSULFATE KINASE;
COMPND 6 EC: 2.7.1.25;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SYNECHOCYSTIS SP. (STRAIN PCC 6803 / KAZUSA);
SOURCE 3 ORGANISM_TAXID: 1111708;
SOURCE 4 STRAIN: PCC 6803 / KAZUSA;
SOURCE 5 GENE: CYSC, SLR0676;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)
KEYWDS SYNECHOCYSTIS, SULFUR METABOLISM, KINASE, TRANSFERASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.HERRMANN,J.M.JEZ
REVDAT 3 27-SEP-23 5CB8 1 JRNL REMARK
REVDAT 2 28-OCT-15 5CB8 1 JRNL
REVDAT 1 02-SEP-15 5CB8 0
JRNL AUTH J.HERRMANN,D.NATHIN,S.G.LEE,T.SUN,J.M.JEZ
JRNL TITL RECAPITULATING THE STRUCTURAL EVOLUTION OF REDOX REGULATION
JRNL TITL 2 IN ADENOSINE 5'-PHOSPHOSULFATE KINASE FROM CYANOBACTERIA TO
JRNL TITL 3 PLANTS.
JRNL REF J.BIOL.CHEM. V. 290 24705 2015
JRNL REFN ESSN 1083-351X
JRNL PMID 26294763
JRNL DOI 10.1074/JBC.M115.679514
REMARK 2
REMARK 2 RESOLUTION. 1.88 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.8.1_1168
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) : 1.88
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 31.47
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 3 NUMBER OF REFLECTIONS : 37755
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.156
REMARK 3 R VALUE (WORKING SET) : 0.155
REMARK 3 FREE R VALUE : 0.176
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 1891
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 31.4784 - 4.5267 1.00 2665 137 0.1706 0.1675
REMARK 3 2 4.5267 - 3.5946 1.00 2592 132 0.1262 0.1365
REMARK 3 3 3.5946 - 3.1407 1.00 2582 137 0.1477 0.1456
REMARK 3 4 3.1407 - 2.8538 1.00 2568 126 0.1564 0.1919
REMARK 3 5 2.8538 - 2.6493 1.00 2543 135 0.1581 0.1816
REMARK 3 6 2.6493 - 2.4932 1.00 2571 127 0.1582 0.1751
REMARK 3 7 2.4932 - 2.3684 1.00 2573 124 0.1557 0.1717
REMARK 3 8 2.3684 - 2.2653 1.00 2527 145 0.1617 0.1926
REMARK 3 9 2.2653 - 2.1781 1.00 2521 153 0.1535 0.2005
REMARK 3 10 2.1781 - 2.1030 1.00 2513 143 0.1618 0.2028
REMARK 3 11 2.1030 - 2.0372 1.00 2581 128 0.1639 0.2210
REMARK 3 12 2.0372 - 1.9790 1.00 2509 143 0.1650 0.2487
REMARK 3 13 1.9790 - 1.9269 1.00 2563 123 0.1778 0.2025
REMARK 3 14 1.9269 - 1.8799 1.00 2556 138 0.1919 0.2498
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) : 0.180
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 18.080
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 : 0.006 2925
REMARK 3 ANGLE : 1.038 3986
REMARK 3 CHIRALITY : 0.072 456
REMARK 3 PLANARITY : 0.005 505
REMARK 3 DIHEDRAL : 17.572 1145
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN A AND RESID 3:35
REMARK 3 ORIGIN FOR THE GROUP (A): 52.8336 21.8494 5.1370
REMARK 3 T TENSOR
REMARK 3 T11: 0.2430 T22: 0.2413
REMARK 3 T33: 0.1929 T12: 0.0746
REMARK 3 T13: 0.0200 T23: -0.0166
REMARK 3 L TENSOR
REMARK 3 L11: 2.7967 L22: 1.5396
REMARK 3 L33: 1.8552 L12: 1.0651
REMARK 3 L13: -1.0999 L23: -0.2560
REMARK 3 S TENSOR
REMARK 3 S11: -0.0607 S12: 0.0071 S13: -0.2481
REMARK 3 S21: -0.1031 S22: 0.0337 S23: -0.4176
REMARK 3 S31: 0.3008 S32: 0.4397 S33: 0.0863
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN A AND RESID 36:103
REMARK 3 ORIGIN FOR THE GROUP (A): 45.8880 31.5895 12.4075
REMARK 3 T TENSOR
REMARK 3 T11: 0.1690 T22: 0.1475
REMARK 3 T33: 0.1422 T12: 0.0170
REMARK 3 T13: -0.0132 T23: -0.0104
REMARK 3 L TENSOR
REMARK 3 L11: 2.2462 L22: 1.1990
REMARK 3 L33: 1.0687 L12: 0.9642
REMARK 3 L13: -0.4310 L23: -0.3236
REMARK 3 S TENSOR
REMARK 3 S11: 0.0075 S12: -0.0051 S13: 0.1124
REMARK 3 S21: -0.0056 S22: -0.0158 S23: -0.0543
REMARK 3 S31: 0.0492 S32: 0.0869 S33: 0.0206
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN A AND RESID 104:176
REMARK 3 ORIGIN FOR THE GROUP (A): 40.0880 18.4062 5.5700
REMARK 3 T TENSOR
REMARK 3 T11: 0.2418 T22: 0.1532
REMARK 3 T33: 0.1354 T12: 0.0124
REMARK 3 T13: -0.0076 T23: -0.0081
REMARK 3 L TENSOR
REMARK 3 L11: 1.2924 L22: 1.1806
REMARK 3 L33: 1.7569 L12: 0.8226
REMARK 3 L13: -0.5324 L23: -0.3037
REMARK 3 S TENSOR
REMARK 3 S11: -0.1221 S12: 0.0980 S13: -0.0785
REMARK 3 S21: -0.2340 S22: 0.0659 S23: -0.0661
REMARK 3 S31: 0.2303 S32: 0.0065 S33: 0.0405
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN B AND RESID 2:35
REMARK 3 ORIGIN FOR THE GROUP (A): 65.5874 48.1713 17.0990
REMARK 3 T TENSOR
REMARK 3 T11: 0.1983 T22: 0.2571
REMARK 3 T33: 0.2637 T12: -0.0197
REMARK 3 T13: 0.0353 T23: 0.0793
REMARK 3 L TENSOR
REMARK 3 L11: 1.8673 L22: 1.3833
REMARK 3 L33: 2.8666 L12: -0.1009
REMARK 3 L13: -1.0700 L23: 0.6985
REMARK 3 S TENSOR
REMARK 3 S11: -0.0009 S12: 0.4465 S13: 0.2920
REMARK 3 S21: -0.4086 S22: 0.0389 S23: -0.1604
REMARK 3 S31: -0.1732 S32: 0.0295 S33: -0.1182
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN B AND RESID 36:103
REMARK 3 ORIGIN FOR THE GROUP (A): 58.0018 38.8402 24.4345
REMARK 3 T TENSOR
REMARK 3 T11: 0.1487 T22: 0.1374
REMARK 3 T33: 0.1725 T12: -0.0058
REMARK 3 T13: -0.0086 T23: 0.0172
REMARK 3 L TENSOR
REMARK 3 L11: 1.2259 L22: 1.0593
REMARK 3 L33: 2.4083 L12: -0.3292
REMARK 3 L13: -0.2218 L23: 1.0842
REMARK 3 S TENSOR
REMARK 3 S11: 0.0077 S12: 0.0774 S13: 0.0728
REMARK 3 S21: -0.0533 S22: 0.0044 S23: -0.0563
REMARK 3 S31: 0.1271 S32: -0.0071 S33: -0.0133
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN B AND RESID 104:177
REMARK 3 ORIGIN FOR THE GROUP (A): 64.8313 51.9425 30.1603
REMARK 3 T TENSOR
REMARK 3 T11: 0.1359 T22: 0.1551
REMARK 3 T33: 0.2456 T12: -0.0155
REMARK 3 T13: -0.0033 T23: 0.0123
REMARK 3 L TENSOR
REMARK 3 L11: 1.6798 L22: 1.1695
REMARK 3 L33: 1.2782 L12: -0.2486
REMARK 3 L13: -0.4556 L23: 0.8436
REMARK 3 S TENSOR
REMARK 3 S11: 0.0374 S12: 0.0041 S13: 0.2465
REMARK 3 S21: -0.0616 S22: 0.0764 S23: -0.2441
REMARK 3 S31: -0.0890 S32: 0.1263 S33: -0.0792
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 5CB8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-JUL-15.
REMARK 100 THE DEPOSITION ID IS D_1000211336.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 12-DEC-12
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 10.5
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 19-BM
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.98
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : SBC-3
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000
REMARK 200 DATA SCALING SOFTWARE : HKL-3000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 37779
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.880
REMARK 200 RESOLUTION RANGE LOW (A) : 31.500
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 100.0
REMARK 200 DATA REDUNDANCY : 21.40
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 50.0000
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: PHENIX 1.8.1_1168
REMARK 200 STARTING MODEL: 5CB6
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.29
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.95
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 5 MM APS AND 10 MM K2SO4 AND MIXED
REMARK 280 WITH 0.1 M CAPS/KOH, PH 10.5, 2 M AMMONIUM SULFATE, AND 0.2 M
REMARK 280 LISO4, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 3
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z
REMARK 290 3555 -X,Y,-Z
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 Z,X,Y
REMARK 290 6555 Z,-X,-Y
REMARK 290 7555 -Z,-X,Y
REMARK 290 8555 -Z,X,-Y
REMARK 290 9555 Y,Z,X
REMARK 290 10555 -Y,Z,-X
REMARK 290 11555 Y,-Z,-X
REMARK 290 12555 -Y,-Z,X
REMARK 290 13555 X+1/2,Y+1/2,Z+1/2
REMARK 290 14555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 15555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 16555 X+1/2,-Y+1/2,-Z+1/2
REMARK 290 17555 Z+1/2,X+1/2,Y+1/2
REMARK 290 18555 Z+1/2,-X+1/2,-Y+1/2
REMARK 290 19555 -Z+1/2,-X+1/2,Y+1/2
REMARK 290 20555 -Z+1/2,X+1/2,-Y+1/2
REMARK 290 21555 Y+1/2,Z+1/2,X+1/2
REMARK 290 22555 -Y+1/2,Z+1/2,-X+1/2
REMARK 290 23555 Y+1/2,-Z+1/2,-X+1/2
REMARK 290 24555 -Y+1/2,-Z+1/2,X+1/2
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 6 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY2 6 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 7 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY2 8 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY1 9 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 9 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 9 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 10 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 10 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY3 10 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 11 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 11 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 11 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 12 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 12 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY3 12 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY1 13 1.000000 0.000000 0.000000 70.37800
REMARK 290 SMTRY2 13 0.000000 1.000000 0.000000 70.37800
REMARK 290 SMTRY3 13 0.000000 0.000000 1.000000 70.37800
REMARK 290 SMTRY1 14 -1.000000 0.000000 0.000000 70.37800
REMARK 290 SMTRY2 14 0.000000 -1.000000 0.000000 70.37800
REMARK 290 SMTRY3 14 0.000000 0.000000 1.000000 70.37800
REMARK 290 SMTRY1 15 -1.000000 0.000000 0.000000 70.37800
REMARK 290 SMTRY2 15 0.000000 1.000000 0.000000 70.37800
REMARK 290 SMTRY3 15 0.000000 0.000000 -1.000000 70.37800
REMARK 290 SMTRY1 16 1.000000 0.000000 0.000000 70.37800
REMARK 290 SMTRY2 16 0.000000 -1.000000 0.000000 70.37800
REMARK 290 SMTRY3 16 0.000000 0.000000 -1.000000 70.37800
REMARK 290 SMTRY1 17 0.000000 0.000000 1.000000 70.37800
REMARK 290 SMTRY2 17 1.000000 0.000000 0.000000 70.37800
REMARK 290 SMTRY3 17 0.000000 1.000000 0.000000 70.37800
REMARK 290 SMTRY1 18 0.000000 0.000000 1.000000 70.37800
REMARK 290 SMTRY2 18 -1.000000 0.000000 0.000000 70.37800
REMARK 290 SMTRY3 18 0.000000 -1.000000 0.000000 70.37800
REMARK 290 SMTRY1 19 0.000000 0.000000 -1.000000 70.37800
REMARK 290 SMTRY2 19 -1.000000 0.000000 0.000000 70.37800
REMARK 290 SMTRY3 19 0.000000 1.000000 0.000000 70.37800
REMARK 290 SMTRY1 20 0.000000 0.000000 -1.000000 70.37800
REMARK 290 SMTRY2 20 1.000000 0.000000 0.000000 70.37800
REMARK 290 SMTRY3 20 0.000000 -1.000000 0.000000 70.37800
REMARK 290 SMTRY1 21 0.000000 1.000000 0.000000 70.37800
REMARK 290 SMTRY2 21 0.000000 0.000000 1.000000 70.37800
REMARK 290 SMTRY3 21 1.000000 0.000000 0.000000 70.37800
REMARK 290 SMTRY1 22 0.000000 -1.000000 0.000000 70.37800
REMARK 290 SMTRY2 22 0.000000 0.000000 1.000000 70.37800
REMARK 290 SMTRY3 22 -1.000000 0.000000 0.000000 70.37800
REMARK 290 SMTRY1 23 0.000000 1.000000 0.000000 70.37800
REMARK 290 SMTRY2 23 0.000000 0.000000 -1.000000 70.37800
REMARK 290 SMTRY3 23 -1.000000 0.000000 0.000000 70.37800
REMARK 290 SMTRY1 24 0.000000 -1.000000 0.000000 70.37800
REMARK 290 SMTRY2 24 0.000000 0.000000 -1.000000 70.37800
REMARK 290 SMTRY3 24 1.000000 0.000000 0.000000 70.37800
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4010 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 15700 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -85.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 -19
REMARK 465 GLY A -18
REMARK 465 SER A -17
REMARK 465 SER A -16
REMARK 465 HIS A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 SER A -9
REMARK 465 SER A -8
REMARK 465 GLY A -7
REMARK 465 LEU A -6
REMARK 465 VAL A -5
REMARK 465 PRO A -4
REMARK 465 ARG A -3
REMARK 465 GLY A -2
REMARK 465 SER A -1
REMARK 465 HIS A 0
REMARK 465 MET A 1
REMARK 465 GLN A 2
REMARK 465 GLY A 177
REMARK 465 MET B -19
REMARK 465 GLY B -18
REMARK 465 SER B -17
REMARK 465 SER B -16
REMARK 465 HIS B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 SER B -9
REMARK 465 SER B -8
REMARK 465 GLY B -7
REMARK 465 LEU B -6
REMARK 465 VAL B -5
REMARK 465 PRO B -4
REMARK 465 ARG B -3
REMARK 465 GLY B -2
REMARK 465 SER B -1
REMARK 465 HIS B 0
REMARK 465 MET B 1
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 558 O HOH A 589 1.82
REMARK 500 O HOH B 456 O HOH B 555 1.84
REMARK 500 O HOH A 479 O HOH A 555 1.85
REMARK 500 O HOH B 559 O HOH B 589 1.86
REMARK 500 O HOH A 592 O HOH A 623 1.89
REMARK 500 O HOH A 580 O HOH A 671 1.90
REMARK 500 O HOH A 452 O HOH B 512 1.91
REMARK 500 O HOH A 627 O HOH A 680 1.92
REMARK 500 O HOH A 652 O HOH A 660 1.93
REMARK 500 O HOH A 406 O HOH A 571 1.95
REMARK 500 O HOH A 612 O HOH A 623 1.97
REMARK 500 O HOH A 526 O HOH B 472 2.00
REMARK 500 O HOH B 597 O HOH B 629 2.00
REMARK 500 O HOH B 401 O HOH B 571 2.07
REMARK 500 O HOH B 624 O HOH B 629 2.08
REMARK 500 O HOH B 613 O HOH B 659 2.09
REMARK 500 O HOH A 457 O HOH A 646 2.10
REMARK 500 O HOH B 436 O HOH B 634 2.12
REMARK 500 OE1 GLN B 2 O HOH B 401 2.12
REMARK 500 O HOH A 566 O HOH A 619 2.14
REMARK 500 O HOH B 571 O HOH B 661 2.17
REMARK 500 O HOH B 582 O HOH B 618 2.17
REMARK 500 O HOH A 516 O HOH A 593 2.19
REMARK 500 O HOH B 621 O HOH B 662 2.19
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: CLOSE CONTACTS
REMARK 500
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT. AN ATOM LOCATED WITHIN 0.15
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375
REMARK 500 INSTEAD OF REMARK 500. ATOMS WITH NON-BLANK ALTERNATE
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.
REMARK 500
REMARK 500 DISTANCE CUTOFF:
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS
REMARK 500
REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI SSYMOP DISTANCE
REMARK 500 O HOH A 508 O HOH A 584 9555 1.84
REMARK 500 O HOH B 505 O HOH B 572 5555 2.02
REMARK 500 O HOH A 469 O HOH B 603 24554 2.03
REMARK 500 O HOH A 615 O HOH B 513 24554 2.17
REMARK 500 O HOH A 636 O HOH A 673 5555 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 47 -87.37 -137.60
REMARK 500 ASN A 47 -86.85 -137.89
REMARK 500 SER A 86 66.32 39.19
REMARK 500 ASP A 118 59.50 38.76
REMARK 500 ASN A 146 58.24 -143.76
REMARK 500 ASN B 47 -88.37 -136.51
REMARK 500 SER B 86 65.86 38.05
REMARK 500 ASP B 118 58.24 38.24
REMARK 500 ASN B 146 58.80 -141.88
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 A 692 DISTANCE = 6.32 ANGSTROMS
REMARK 525 HOH B 665 DISTANCE = 6.54 ANGSTROMS
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ADX A 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 A 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT A 304
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ADX B 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 302
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 B 303
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT B 304
DBREF 5CB8 A 1 177 UNP P72940 CYSC_SYNY3 1 177
DBREF 5CB8 B 1 177 UNP P72940 CYSC_SYNY3 1 177
SEQADV 5CB8 MET A -19 UNP P72940 INITIATING METHIONINE
SEQADV 5CB8 GLY A -18 UNP P72940 EXPRESSION TAG
SEQADV 5CB8 SER A -17 UNP P72940 EXPRESSION TAG
SEQADV 5CB8 SER A -16 UNP P72940 EXPRESSION TAG
SEQADV 5CB8 HIS A -15 UNP P72940 EXPRESSION TAG
SEQADV 5CB8 HIS A -14 UNP P72940 EXPRESSION TAG
SEQADV 5CB8 HIS A -13 UNP P72940 EXPRESSION TAG
SEQADV 5CB8 HIS A -12 UNP P72940 EXPRESSION TAG
SEQADV 5CB8 HIS A -11 UNP P72940 EXPRESSION TAG
SEQADV 5CB8 HIS A -10 UNP P72940 EXPRESSION TAG
SEQADV 5CB8 SER A -9 UNP P72940 EXPRESSION TAG
SEQADV 5CB8 SER A -8 UNP P72940 EXPRESSION TAG
SEQADV 5CB8 GLY A -7 UNP P72940 EXPRESSION TAG
SEQADV 5CB8 LEU A -6 UNP P72940 EXPRESSION TAG
SEQADV 5CB8 VAL A -5 UNP P72940 EXPRESSION TAG
SEQADV 5CB8 PRO A -4 UNP P72940 EXPRESSION TAG
SEQADV 5CB8 ARG A -3 UNP P72940 EXPRESSION TAG
SEQADV 5CB8 GLY A -2 UNP P72940 EXPRESSION TAG
SEQADV 5CB8 SER A -1 UNP P72940 EXPRESSION TAG
SEQADV 5CB8 HIS A 0 UNP P72940 EXPRESSION TAG
SEQADV 5CB8 MET B -19 UNP P72940 INITIATING METHIONINE
SEQADV 5CB8 GLY B -18 UNP P72940 EXPRESSION TAG
SEQADV 5CB8 SER B -17 UNP P72940 EXPRESSION TAG
SEQADV 5CB8 SER B -16 UNP P72940 EXPRESSION TAG
SEQADV 5CB8 HIS B -15 UNP P72940 EXPRESSION TAG
SEQADV 5CB8 HIS B -14 UNP P72940 EXPRESSION TAG
SEQADV 5CB8 HIS B -13 UNP P72940 EXPRESSION TAG
SEQADV 5CB8 HIS B -12 UNP P72940 EXPRESSION TAG
SEQADV 5CB8 HIS B -11 UNP P72940 EXPRESSION TAG
SEQADV 5CB8 HIS B -10 UNP P72940 EXPRESSION TAG
SEQADV 5CB8 SER B -9 UNP P72940 EXPRESSION TAG
SEQADV 5CB8 SER B -8 UNP P72940 EXPRESSION TAG
SEQADV 5CB8 GLY B -7 UNP P72940 EXPRESSION TAG
SEQADV 5CB8 LEU B -6 UNP P72940 EXPRESSION TAG
SEQADV 5CB8 VAL B -5 UNP P72940 EXPRESSION TAG
SEQADV 5CB8 PRO B -4 UNP P72940 EXPRESSION TAG
SEQADV 5CB8 ARG B -3 UNP P72940 EXPRESSION TAG
SEQADV 5CB8 GLY B -2 UNP P72940 EXPRESSION TAG
SEQADV 5CB8 SER B -1 UNP P72940 EXPRESSION TAG
SEQADV 5CB8 HIS B 0 UNP P72940 EXPRESSION TAG
SEQRES 1 A 197 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 197 LEU VAL PRO ARG GLY SER HIS MET GLN GLN ARG GLY VAL
SEQRES 3 A 197 THR ILE TRP LEU THR GLY LEU SER GLY ALA GLY LYS THR
SEQRES 4 A 197 THR ILE THR HIS ALA LEU GLU LYS LYS LEU ARG ASP SER
SEQRES 5 A 197 GLY TYR ARG LEU GLU VAL LEU ASP GLY ASP VAL VAL ARG
SEQRES 6 A 197 THR ASN LEU THR LYS GLY LEU GLY PHE SER LYS GLU ASP
SEQRES 7 A 197 ARG ASP THR ASN ILE ARG ARG ILE GLY PHE VAL SER HIS
SEQRES 8 A 197 LEU LEU THR ARG ASN GLY VAL ILE VAL LEU VAL SER ALA
SEQRES 9 A 197 ILE SER PRO TYR ALA ALA ILE ARG GLN GLU VAL LYS HIS
SEQRES 10 A 197 THR ILE GLY ASP PHE LEU GLU VAL PHE VAL ASN ALA PRO
SEQRES 11 A 197 LEU ALA VAL CYS GLU GLU ARG ASP VAL LYS GLY LEU TYR
SEQRES 12 A 197 ALA LYS ALA ARG SER GLY GLU ILE LYS GLY PHE THR GLY
SEQRES 13 A 197 ILE ASP ASP PRO TYR GLU PRO PRO THR ASN PRO ASP VAL
SEQRES 14 A 197 GLU CYS ARG THR ASP LEU GLU GLU LEU ASP GLU SER VAL
SEQRES 15 A 197 GLY LYS ILE TRP GLN LYS LEU VAL ASP LEU LYS TYR ILE
SEQRES 16 A 197 GLU GLY
SEQRES 1 B 197 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 197 LEU VAL PRO ARG GLY SER HIS MET GLN GLN ARG GLY VAL
SEQRES 3 B 197 THR ILE TRP LEU THR GLY LEU SER GLY ALA GLY LYS THR
SEQRES 4 B 197 THR ILE THR HIS ALA LEU GLU LYS LYS LEU ARG ASP SER
SEQRES 5 B 197 GLY TYR ARG LEU GLU VAL LEU ASP GLY ASP VAL VAL ARG
SEQRES 6 B 197 THR ASN LEU THR LYS GLY LEU GLY PHE SER LYS GLU ASP
SEQRES 7 B 197 ARG ASP THR ASN ILE ARG ARG ILE GLY PHE VAL SER HIS
SEQRES 8 B 197 LEU LEU THR ARG ASN GLY VAL ILE VAL LEU VAL SER ALA
SEQRES 9 B 197 ILE SER PRO TYR ALA ALA ILE ARG GLN GLU VAL LYS HIS
SEQRES 10 B 197 THR ILE GLY ASP PHE LEU GLU VAL PHE VAL ASN ALA PRO
SEQRES 11 B 197 LEU ALA VAL CYS GLU GLU ARG ASP VAL LYS GLY LEU TYR
SEQRES 12 B 197 ALA LYS ALA ARG SER GLY GLU ILE LYS GLY PHE THR GLY
SEQRES 13 B 197 ILE ASP ASP PRO TYR GLU PRO PRO THR ASN PRO ASP VAL
SEQRES 14 B 197 GLU CYS ARG THR ASP LEU GLU GLU LEU ASP GLU SER VAL
SEQRES 15 B 197 GLY LYS ILE TRP GLN LYS LEU VAL ASP LEU LYS TYR ILE
SEQRES 16 B 197 GLU GLY
HET ADX A 301 27
HET SO4 A 302 5
HET SO4 A 303 5
HET ACT A 304 4
HET ADX B 301 27
HET SO4 B 302 5
HET SO4 B 303 5
HET ACT B 304 4
HETNAM ADX ADENOSINE-5'-PHOSPHOSULFATE
HETNAM SO4 SULFATE ION
HETNAM ACT ACETATE ION
FORMUL 3 ADX 2(C10 H14 N5 O10 P S)
FORMUL 4 SO4 4(O4 S 2-)
FORMUL 6 ACT 2(C2 H3 O2 1-)
FORMUL 11 HOH *557(H2 O)
HELIX 1 AA1 GLY A 17 SER A 32 1 16
HELIX 2 AA2 GLY A 41 ARG A 45 1 5
HELIX 3 AA3 SER A 55 ARG A 75 1 21
HELIX 4 AA4 TYR A 88 GLY A 100 1 13
HELIX 5 AA5 PRO A 110 ASP A 118 1 9
HELIX 6 AA6 GLY A 121 SER A 128 1 8
HELIX 7 AA7 GLU A 157 LEU A 172 1 16
HELIX 8 AA8 GLY B 17 ASP B 31 1 15
HELIX 9 AA9 GLY B 41 ARG B 45 1 5
HELIX 10 AB1 SER B 55 ARG B 75 1 21
HELIX 11 AB2 TYR B 88 GLY B 100 1 13
HELIX 12 AB3 PRO B 110 ASP B 118 1 9
HELIX 13 AB4 GLY B 121 SER B 128 1 8
HELIX 14 AB5 GLU B 157 LEU B 172 1 16
SHEET 1 AA1 5 LEU A 36 ASP A 40 0
SHEET 2 AA1 5 ILE A 79 SER A 83 1 O LEU A 81 N LEU A 39
SHEET 3 AA1 5 VAL A 6 THR A 11 1 N ILE A 8 O VAL A 80
SHEET 4 AA1 5 PHE A 102 VAL A 107 1 O VAL A 105 N TRP A 9
SHEET 5 AA1 5 VAL A 149 CYS A 151 1 O CYS A 151 N PHE A 106
SHEET 1 AA2 5 LEU B 36 ASP B 40 0
SHEET 2 AA2 5 ILE B 79 SER B 83 1 O LEU B 81 N LEU B 39
SHEET 3 AA2 5 VAL B 6 THR B 11 1 N ILE B 8 O VAL B 80
SHEET 4 AA2 5 PHE B 102 VAL B 107 1 O VAL B 105 N TRP B 9
SHEET 5 AA2 5 VAL B 149 CYS B 151 1 O CYS B 151 N PHE B 106
SITE 1 AC1 19 ASP A 42 ARG A 45 PHE A 54 ARG A 59
SITE 2 AC1 19 ASN A 62 ILE A 63 ALA A 84 ILE A 85
SITE 3 AC1 19 SER A 86 PRO A 87 LYS A 120 LEU A 122
SITE 4 AC1 19 GLY A 133 PHE A 134 THR A 135 HOH A 417
SITE 5 AC1 19 HOH A 429 HOH A 498 HOH A 553
SITE 1 AC2 10 LEU A 13 GLY A 15 ALA A 16 GLY A 17
SITE 2 AC2 10 LYS A 18 THR A 19 HOH A 420 HOH A 421
SITE 3 AC2 10 HOH A 429 HOH A 472
SITE 1 AC3 6 THR A 61 ARG A 64 HOH A 448 HOH A 456
SITE 2 AC3 6 HOH A 475 HOH A 536
SITE 1 AC4 3 HIS A 71 ARG A 75 HOH A 466
SITE 1 AC5 20 ASP B 42 ARG B 45 PHE B 54 ARG B 59
SITE 2 AC5 20 ASN B 62 ILE B 63 ALA B 84 ILE B 85
SITE 3 AC5 20 SER B 86 PRO B 87 LYS B 120 LEU B 122
SITE 4 AC5 20 GLY B 133 PHE B 134 THR B 135 HOH B 413
SITE 5 AC5 20 HOH B 418 HOH B 489 HOH B 496 HOH B 525
SITE 1 AC6 11 LEU B 13 SER B 14 GLY B 15 ALA B 16
SITE 2 AC6 11 GLY B 17 LYS B 18 THR B 19 HOH B 407
SITE 3 AC6 11 HOH B 413 HOH B 424 HOH B 449
SITE 1 AC7 9 LYS A 50 HOH A 452 THR B 61 ARG B 64
SITE 2 AC7 9 HOH B 430 HOH B 447 HOH B 451 HOH B 512
SITE 3 AC7 9 HOH B 546
SITE 1 AC8 3 HIS B 71 ARG B 75 HOH B 501
CRYST1 140.756 140.756 140.756 90.00 90.00 90.00 I 2 3 48
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 0.007104 0.000000 0.000000 0.00000
SCALE2 0.000000 0.007104 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007104 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
