HEADER LIGASE 11-AUG-18 6AGG
TITLE CRYSTAL STRUCTURE OF AGMATINE-AMPPCP-MG COMPLEXED TIAS (TRNAILE2
TITLE 2 AGMATIDINE SYNTHETASE)
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: TRNA(ILE2) 2-AGMATINYLCYTIDINE SYNTHETASE TIAS;
COMPND 3 CHAIN: Z;
COMPND 4 SYNONYM: TRNA(ILE2)-AGM2C SYNTHETASE,TRNA(ILE2) AGMATIDINE
COMPND 5 SYNTHETASE;
COMPND 6 EC: 6.3.4.22;
COMPND 7 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ARCHAEOGLOBUS FULGIDUS (STRAIN ATCC 49558 / VC-
SOURCE 3 16 / DSM 4304 / JCM 9628 / NBRC 100126);
SOURCE 4 ORGANISM_TAXID: 224325;
SOURCE 5 STRAIN: ATCC 49558 / VC-16 / DSM 4304 / JCM 9628 / NBRC 100126;
SOURCE 6 GENE: TIAS, AF_2259;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ZINC RIBBON, CONFORMATIONAL CHANGE, TIAS, TRNA MODIFICATION, ZINC
KEYWDS 2 FINGER ENGINEERING, LIGASE
EXPDTA X-RAY DIFFRACTION
AUTHOR J.S.DONG,W.M.GONG
REVDAT 2 24-OCT-18 6AGG 1 JRNL
REVDAT 1 05-SEP-18 6AGG 0
JRNL AUTH J.DONG,F.LI,F.GAO,J.WEI,Y.LIN,Y.ZHANG,J.LOU,G.LIU,Y.DONG,
JRNL AUTH 2 L.LIU,H.LIU,J.WANG,W.GONG
JRNL TITL STRUCTURE OF TRNA-MODIFYING ENZYME TIAS AND MOTIONS OF ITS
JRNL TITL 2 SUBSTRATE BINDING ZINC RIBBON.
JRNL REF J. MOL. BIOL. V. 430 4183 2018
JRNL REFN ESSN 1089-8638
JRNL PMID 30121296
JRNL DOI 10.1016/J.JMB.2018.08.015
REMARK 2
REMARK 2 RESOLUTION. 2.71 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.7.1_743
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.71
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 29.10
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.9
REMARK 3 NUMBER OF REFLECTIONS : 14667
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.215
REMARK 3 R VALUE (WORKING SET) : 0.211
REMARK 3 FREE R VALUE : 0.298
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010
REMARK 3 FREE R VALUE TEST SET COUNT : 735
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 29.0964 - 4.6229 0.98 2974 138 0.2013 0.2704
REMARK 3 2 4.6229 - 3.6717 0.98 2787 152 0.1977 0.2933
REMARK 3 3 3.6717 - 3.2082 0.99 2782 139 0.2173 0.3237
REMARK 3 4 3.2082 - 2.9152 0.99 2729 153 0.2206 0.3127
REMARK 3 5 2.9152 - 2.7064 0.96 2660 153 0.3114 0.4248
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.00
REMARK 3 SHRINKAGE RADIUS : 0.72
REMARK 3 K_SOL : 0.33
REMARK 3 B_SOL : 67.78
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.760
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.620
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) : 16.67120
REMARK 3 B22 (A**2) : 16.67120
REMARK 3 B33 (A**2) : -33.34250
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 TWINNING INFORMATION.
REMARK 3 FRACTION: NULL
REMARK 3 OPERATOR: NULL
REMARK 3
REMARK 3 DEVIATIONS FROM IDEAL VALUES.
REMARK 3 RMSD COUNT
REMARK 3 BOND : 0.007 3486
REMARK 3 ANGLE : 1.079 4713
REMARK 3 CHIRALITY : 0.073 513
REMARK 3 PLANARITY : 0.004 613
REMARK 3 DIHEDRAL : 16.706 1327
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 10
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'Z' AND (RESSEQ 1:44)
REMARK 3 ORIGIN FOR THE GROUP (A): 8.9348 13.0992 33.5623
REMARK 3 T TENSOR
REMARK 3 T11: 0.7613 T22: 0.3400
REMARK 3 T33: 0.5772 T12: 0.2019
REMARK 3 T13: -0.0658 T23: 0.0405
REMARK 3 L TENSOR
REMARK 3 L11: 4.0370 L22: 4.6433
REMARK 3 L33: 6.7262 L12: 2.0521
REMARK 3 L13: 1.3905 L23: -0.5381
REMARK 3 S TENSOR
REMARK 3 S11: 0.2430 S12: 0.3075 S13: -0.0820
REMARK 3 S21: -0.8248 S22: 0.2863 S23: 0.6936
REMARK 3 S31: -0.3254 S32: -0.0319 S33: -0.3827
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'Z' AND (RESSEQ 45:67)
REMARK 3 ORIGIN FOR THE GROUP (A): 11.0612 6.6215 38.5120
REMARK 3 T TENSOR
REMARK 3 T11: 0.6881 T22: 0.5139
REMARK 3 T33: 0.3683 T12: 0.1460
REMARK 3 T13: 0.1909 T23: 0.0568
REMARK 3 L TENSOR
REMARK 3 L11: 1.9415 L22: 4.9288
REMARK 3 L33: 5.3291 L12: 2.2849
REMARK 3 L13: 0.2843 L23: 0.1719
REMARK 3 S TENSOR
REMARK 3 S11: -0.5270 S12: 1.1813 S13: 0.4973
REMARK 3 S21: -0.0246 S22: 0.1098 S23: -0.8943
REMARK 3 S31: -0.5761 S32: 0.3953 S33: 0.3089
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'Z' AND (RESSEQ 68:128)
REMARK 3 ORIGIN FOR THE GROUP (A): 6.7990 1.4158 34.8482
REMARK 3 T TENSOR
REMARK 3 T11: 0.5983 T22: 0.3623
REMARK 3 T33: 0.5537 T12: 0.1546
REMARK 3 T13: 0.0554 T23: 0.0317
REMARK 3 L TENSOR
REMARK 3 L11: 2.6873 L22: 5.6634
REMARK 3 L33: 7.4287 L12: 1.9206
REMARK 3 L13: -0.6277 L23: -1.0530
REMARK 3 S TENSOR
REMARK 3 S11: -0.0420 S12: 0.0588 S13: -0.4176
REMARK 3 S21: -0.2767 S22: 0.1246 S23: 0.0231
REMARK 3 S31: -0.0127 S32: -0.5229 S33: -0.1890
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'Z' AND (RESSEQ 129:162)
REMARK 3 ORIGIN FOR THE GROUP (A): 8.1129 4.6654 39.2232
REMARK 3 T TENSOR
REMARK 3 T11: 0.5089 T22: 0.4215
REMARK 3 T33: 0.5726 T12: 0.1063
REMARK 3 T13: -0.0131 T23: 0.0145
REMARK 3 L TENSOR
REMARK 3 L11: 2.6379 L22: 5.2730
REMARK 3 L33: 5.5135 L12: 3.2483
REMARK 3 L13: 1.7139 L23: -0.2677
REMARK 3 S TENSOR
REMARK 3 S11: -0.0938 S12: -0.2441 S13: 0.0063
REMARK 3 S21: -0.2507 S22: 0.4576 S23: 0.1998
REMARK 3 S31: -0.0313 S32: -0.1468 S33: -0.1383
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'Z' AND (RESSEQ 163:238)
REMARK 3 ORIGIN FOR THE GROUP (A): 24.8818 23.9148 42.6789
REMARK 3 T TENSOR
REMARK 3 T11: 1.1064 T22: 0.6349
REMARK 3 T33: 0.5790 T12: -0.2559
REMARK 3 T13: -0.1195 T23: 0.0043
REMARK 3 L TENSOR
REMARK 3 L11: 4.6374 L22: 3.4539
REMARK 3 L33: 5.5768 L12: -0.2989
REMARK 3 L13: 0.5068 L23: 0.3283
REMARK 3 S TENSOR
REMARK 3 S11: -0.3624 S12: -0.3282 S13: 0.8988
REMARK 3 S21: 0.4247 S22: 0.0239 S23: -0.3463
REMARK 3 S31: -1.6655 S32: 1.4355 S33: 0.2158
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'Z' AND (RESSEQ 239:264)
REMARK 3 ORIGIN FOR THE GROUP (A): 16.0869 2.4536 52.2419
REMARK 3 T TENSOR
REMARK 3 T11: 0.4818 T22: 0.3679
REMARK 3 T33: 0.4902 T12: 0.1551
REMARK 3 T13: 0.0702 T23: 0.0475
REMARK 3 L TENSOR
REMARK 3 L11: 3.7564 L22: 1.0218
REMARK 3 L33: 4.2221 L12: 0.2698
REMARK 3 L13: -0.0326 L23: 0.7483
REMARK 3 S TENSOR
REMARK 3 S11: 0.2155 S12: -0.4435 S13: -0.6001
REMARK 3 S21: -0.0050 S22: -0.1265 S23: 0.5325
REMARK 3 S31: -0.0112 S32: 0.1734 S33: -0.0500
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'Z' AND (RESSEQ 265:327)
REMARK 3 ORIGIN FOR THE GROUP (A): 32.5332 -1.7970 61.1095
REMARK 3 T TENSOR
REMARK 3 T11: 0.4175 T22: 1.0207
REMARK 3 T33: 0.6650 T12: 0.2452
REMARK 3 T13: -0.1281 T23: 0.5004
REMARK 3 L TENSOR
REMARK 3 L11: 0.5825 L22: 2.0404
REMARK 3 L33: 2.4116 L12: 0.1748
REMARK 3 L13: 0.1035 L23: 0.3854
REMARK 3 S TENSOR
REMARK 3 S11: 0.1862 S12: -1.1358 S13: -0.4956
REMARK 3 S21: 0.1892 S22: -0.2832 S23: -0.8665
REMARK 3 S31: 0.2557 S32: 1.2042 S33: -0.0913
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'Z' AND (RESSEQ 328:353)
REMARK 3 ORIGIN FOR THE GROUP (A): 36.5855 1.0301 73.1399
REMARK 3 T TENSOR
REMARK 3 T11: 0.6808 T22: 1.1767
REMARK 3 T33: 0.7225 T12: 0.2452
REMARK 3 T13: -0.1092 T23: 0.1783
REMARK 3 L TENSOR
REMARK 3 L11: 2.2140 L22: 0.0735
REMARK 3 L33: 1.0859 L12: 0.4264
REMARK 3 L13: 1.5623 L23: 0.2981
REMARK 3 S TENSOR
REMARK 3 S11: 0.2419 S12: -0.5433 S13: 0.0563
REMARK 3 S21: 0.3716 S22: 0.5070 S23: 0.0304
REMARK 3 S31: 0.2496 S32: -0.3613 S33: -0.8680
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'Z' AND (RESSEQ 354:384)
REMARK 3 ORIGIN FOR THE GROUP (A): 57.0748 1.8491 92.1384
REMARK 3 T TENSOR
REMARK 3 T11: 1.0458 T22: 1.1841
REMARK 3 T33: 0.8419 T12: 0.0677
REMARK 3 T13: -0.0502 T23: -0.0368
REMARK 3 L TENSOR
REMARK 3 L11: 4.4025 L22: 4.3025
REMARK 3 L33: 5.8146 L12: -0.1177
REMARK 3 L13: 2.5051 L23: -0.2108
REMARK 3 S TENSOR
REMARK 3 S11: -0.0816 S12: -1.3578 S13: -0.1809
REMARK 3 S21: -0.3777 S22: 0.0803 S23: -1.0966
REMARK 3 S31: 0.2505 S32: -0.8108 S33: -0.2862
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'Z' AND (RESSEQ 385:420)
REMARK 3 ORIGIN FOR THE GROUP (A): 27.3630 12.0083 62.6605
REMARK 3 T TENSOR
REMARK 3 T11: 0.9652 T22: 1.0630
REMARK 3 T33: 0.5989 T12: -0.0892
REMARK 3 T13: -0.0660 T23: 0.0595
REMARK 3 L TENSOR
REMARK 3 L11: 1.8811 L22: 1.6662
REMARK 3 L33: 3.9095 L12: -0.5322
REMARK 3 L13: 2.3183 L23: -1.6581
REMARK 3 S TENSOR
REMARK 3 S11: -0.1332 S12: -0.5842 S13: 0.0083
REMARK 3 S21: 0.3848 S22: 0.0293 S23: -0.1703
REMARK 3 S31: -0.8977 S32: 0.8642 S33: -0.0116
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 6AGG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-AUG-18.
REMARK 100 THE DEPOSITION ID IS D_1300008706.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-NOV-10
REMARK 200 TEMPERATURE (KELVIN) : 80
REMARK 200 PH : 6.7-7.2
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRF
REMARK 200 BEAMLINE : BL17U
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.979
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14875
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 30.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 200 DATA REDUNDANCY : 27.30
REMARK 200 R MERGE (I) : 0.12300
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 24.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.80
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 28.60
REMARK 200 R MERGE FOR SHELL (I) : 0.55900
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 11.00
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 53.64
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.65
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 50MM HEPES-NA PH7.0-7.2, 0.5M NH4AC,
REMARK 280 0.2M MGCL2, 1.5-2.5% PEG 8000, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4
REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4
REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4
REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4
REMARK 290 7555 Y,X,-Z
REMARK 290 8555 -Y,-X,-Z+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 105.41100
REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 34.89300
REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 34.89300
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 52.70550
REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 34.89300
REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 34.89300
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 158.11650
REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 34.89300
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 34.89300
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 52.70550
REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 34.89300
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 34.89300
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 158.11650
REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 105.41100
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: 1200 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 20220 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: Z
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 TYR Z 51 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS Z 52 CG CD CE NZ
REMARK 470 THR Z 53 OG1 CG2
REMARK 470 ARG Z 54 CG CD NE CZ NH1 NH2
REMARK 470 LYS Z 89 CG CD CE NZ
REMARK 470 ARG Z 270 CG CD NE CZ NH1 NH2
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 ASP Z 8 -169.43 -169.00
REMARK 500 THR Z 19 -49.69 109.44
REMARK 500 TYR Z 51 9.47 100.42
REMARK 500 LYS Z 52 -86.49 -78.19
REMARK 500 ASN Z 56 72.97 -155.09
REMARK 500 ASP Z 115 -156.37 -127.85
REMARK 500 LYS Z 137 -110.34 -140.33
REMARK 500 PHE Z 169 135.73 149.78
REMARK 500 SER Z 179 -36.70 -37.26
REMARK 500 ASP Z 200 50.09 33.67
REMARK 500 PRO Z 209 32.51 -81.37
REMARK 500 PRO Z 235 127.13 -28.93
REMARK 500 ASP Z 237 -74.44 -91.52
REMARK 500 TYR Z 264 28.90 82.57
REMARK 500 THR Z 274 -79.47 -96.95
REMARK 500 GLU Z 281 -76.02 -49.69
REMARK 500 LYS Z 305 -113.86 61.42
REMARK 500 LEU Z 313 40.35 -82.07
REMARK 500 LYS Z 316 134.74 -38.36
REMARK 500 VAL Z 339 -85.18 -78.47
REMARK 500 SER Z 354 -71.95 -84.66
REMARK 500 ARG Z 364 -99.30 -30.05
REMARK 500 LYS Z 371 -39.98 -35.90
REMARK 500 ARG Z 374 42.24 -93.31
REMARK 500 PRO Z 391 172.80 -54.15
REMARK 500 VAL Z 413 161.50 -28.40
REMARK 500 HIS Z 417 77.50 -106.31
REMARK 500
REMARK 500 REMARK: NULL
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 MG Z 508 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP Z 8 OD2
REMARK 620 2 TPO Z 18 O2P 134.4
REMARK 620 3 GLY Z 57 O 124.5 85.4
REMARK 620 4 ACP Z 502 O1B 135.9 84.6 67.3
REMARK 620 5 ACP Z 502 O2A 83.2 77.6 151.5 88.2
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG Z 507 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP Z 11 OD2
REMARK 620 2 TPO Z 18 O1P 56.3
REMARK 620 3 TPO Z 18 O2P 107.2 55.5
REMARK 620 4 ACP Z 502 O1A 94.3 127.6 107.8
REMARK 620 5 ACP Z 502 O2A 135.5 120.0 68.9 50.3
REMARK 620 N 1 2 3 4
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN Z 501 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS Z 352 SG
REMARK 620 2 CYS Z 355 SG 83.1
REMARK 620 3 CYS Z 370 SG 85.1 93.3
REMARK 620 4 CYS Z 373 SG 114.2 148.8 113.1
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN Z 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACP Z 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue AG2 Z 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT Z 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ACT Z 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NH4 Z 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG Z 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG Z 508
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5XOB RELATED DB: PDB
DBREF 6AGG Z 1 420 UNP O28025 TIAS_ARCFU 1 420
SEQRES 1 Z 420 MET ARG VAL TRP VAL GLY ILE ASP ASP THR ASP SER SER
SEQRES 2 Z 420 ARG GLY MET CYS TPO THR TYR LEU ALA VAL LEU ALA MET
SEQRES 3 Z 420 GLU ARG VAL GLU ARG GLU LEU GLY LYS VAL ILE GLY PHE
SEQRES 4 Z 420 PRO ARG LEU ILE ARG LEU ASN PRO THR ILE PRO TYR LYS
SEQRES 5 Z 420 THR ARG GLY ASN GLY ALA VAL SER PHE LEU VAL GLU VAL
SEQRES 6 Z 420 ASP ASP VAL GLY GLU LEU VAL ASP VAL VAL ASN GLU VAL
SEQRES 7 Z 420 ILE ILE GLU HIS ALA MET LEU ASP ASP GLU LYS THR ASN
SEQRES 8 Z 420 PRO GLY ALA VAL PHE VAL ASP GLU GLU LEU ALA VAL LYS
SEQRES 9 Z 420 LEU LYS PRO PHE ALA ASP LYS ALA ILE LYS ASP VAL LEU
SEQRES 10 Z 420 GLN ILE ASP GLU ALA LEU PHE VAL ILE GLY LYS TYR PHE
SEQRES 11 Z 420 ILE PRO HIS LEU ARG HIS LYS LYS GLY ARG GLY LEU ILE
SEQRES 12 Z 420 GLY ALA LEU ALA ALA VAL GLY ALA GLU LEU GLU ASP PHE
SEQRES 13 Z 420 THR LEU GLU LEU ILE ALA TYR ARG TYR PRO GLU ARG PHE
SEQRES 14 Z 420 GLY THR GLU ARG GLU TYR ASP GLU GLU SER PHE PHE ASP
SEQRES 15 Z 420 MET ASP TYR GLU LEU TYR PRO GLN THR PHE ASP ASN VAL
SEQRES 16 Z 420 ASP TRP CYS ASN ASP VAL VAL VAL CYS ILE PRO ASN THR
SEQRES 17 Z 420 PRO CYS PRO VAL LEU TYR GLY ILE ARG GLY GLU SER VAL
SEQRES 18 Z 420 GLU ALA LEU TYR LYS ALA MET GLU SER VAL LYS THR GLU
SEQRES 19 Z 420 PRO VAL ASP ARG ARG MET ILE PHE VAL THR ASN HIS ALA
SEQRES 20 Z 420 THR ASP MET HIS LEU ILE GLY GLU GLU GLU VAL HIS ARG
SEQRES 21 Z 420 LEU GLU ASN TYR ARG SER TYR ARG LEU ARG GLY ARG VAL
SEQRES 22 Z 420 THR LEU GLU PRO TYR ASP ILE GLU GLY GLY HIS VAL PHE
SEQRES 23 Z 420 PHE GLU ILE ASP THR LYS PHE GLY SER VAL LYS CYS ALA
SEQRES 24 Z 420 ALA PHE GLU PRO THR LYS GLN PHE ARG ASN VAL ILE ARG
SEQRES 25 Z 420 LEU LEU ARG LYS GLY ASP VAL VAL GLU VAL TYR GLY SER
SEQRES 26 Z 420 MET LYS LYS ASP THR ILE ASN LEU GLU LYS ILE GLN ILE
SEQRES 27 Z 420 VAL GLU LEU ALA GLU ILE TRP VAL GLU LYS ASN PRO ILE
SEQRES 28 Z 420 CYS PRO SER CYS GLY ARG ARG MET GLU SER ALA GLY ARG
SEQRES 29 Z 420 GLY GLN GLY PHE ARG CYS LYS LYS CYS ARG THR LYS ALA
SEQRES 30 Z 420 ASP GLU LYS LEU ARG GLU LYS VAL GLU ARG GLU LEU GLN
SEQRES 31 Z 420 PRO GLY PHE TYR GLU VAL PRO PRO SER ALA ARG ARG HIS
SEQRES 32 Z 420 LEU SER LYS PRO LEU ILE ARG MET ASN VAL GLU GLY ARG
SEQRES 33 Z 420 HIS ILE PHE ARG
MODRES 6AGG TPO Z 18 THR MODIFIED RESIDUE
HET TPO Z 18 11
HET ZN Z 501 1
HET ACP Z 502 31
HET AG2 Z 503 9
HET ACT Z 504 4
HET ACT Z 505 4
HET NH4 Z 506 1
HET MG Z 507 1
HET MG Z 508 1
HETNAM TPO PHOSPHOTHREONINE
HETNAM ZN ZINC ION
HETNAM ACP PHOSPHOMETHYLPHOSPHONIC ACID ADENYLATE ESTER
HETNAM AG2 AGMATINE
HETNAM ACT ACETATE ION
HETNAM NH4 AMMONIUM ION
HETNAM MG MAGNESIUM ION
HETSYN TPO PHOSPHONOTHREONINE
HETSYN ACP ADENOSINE-5'-[BETA, GAMMA-METHYLENE]TRIPHOSPHATE
HETSYN AG2 (4-AMINOBUTYL)GUANIDINE
FORMUL 1 TPO C4 H10 N O6 P
FORMUL 2 ZN ZN 2+
FORMUL 3 ACP C11 H18 N5 O12 P3
FORMUL 4 AG2 C5 H14 N4
FORMUL 5 ACT 2(C2 H3 O2 1-)
FORMUL 7 NH4 H4 N 1+
FORMUL 8 MG 2(MG 2+)
FORMUL 10 HOH *8(H2 O)
HELIX 1 AA1 THR Z 19 LEU Z 33 1 15
HELIX 2 AA2 ASP Z 67 ALA Z 83 1 17
HELIX 3 AA3 GLU Z 99 VAL Z 103 1 5
HELIX 4 AA4 LEU Z 105 ASP Z 115 1 11
HELIX 5 AA5 GLN Z 118 TYR Z 129 1 12
HELIX 6 AA6 ARG Z 140 ALA Z 151 1 12
HELIX 7 AA7 ASP Z 176 TYR Z 188 1 13
HELIX 8 AA8 SER Z 220 VAL Z 231 1 12
HELIX 9 AA9 GLU Z 256 VAL Z 258 5 3
HELIX 10 AB1 PHE Z 301 LYS Z 305 5 5
HELIX 11 AB2 GLN Z 306 LEU Z 313 1 8
HELIX 12 AB3 PRO Z 397 ARG Z 401 5 5
HELIX 13 AB4 PRO Z 407 MET Z 411 5 5
SHEET 1 AA1 8 HIS Z 133 ARG Z 135 0
SHEET 2 AA1 8 GLY Z 93 ASP Z 98 -1 N ALA Z 94 O LEU Z 134
SHEET 3 AA1 8 ARG Z 2 ASP Z 8 -1 N TRP Z 4 O VAL Z 97
SHEET 4 AA1 8 GLY Z 57 GLU Z 64 -1 O VAL Z 59 N ILE Z 7
SHEET 5 AA1 8 LYS Z 35 ARG Z 44 -1 N ARG Z 41 O SER Z 60
SHEET 6 AA1 8 ARG Z 239 THR Z 244 1 O VAL Z 243 N LEU Z 42
SHEET 7 AA1 8 THR Z 157 TYR Z 163 -1 N THR Z 157 O THR Z 244
SHEET 8 AA1 8 VAL Z 212 GLY Z 218 -1 O TYR Z 214 N ALA Z 162
SHEET 1 AA2 2 VAL Z 195 ASP Z 196 0
SHEET 2 AA2 2 VAL Z 201 VAL Z 202 -1 O VAL Z 201 N ASP Z 196
SHEET 1 AA3 5 LEU Z 252 GLY Z 254 0
SHEET 2 AA3 5 ARG Z 265 VAL Z 273 1 O SER Z 266 N ILE Z 253
SHEET 3 AA3 5 VAL Z 319 LYS Z 327 -1 O MET Z 326 N ARG Z 265
SHEET 4 AA3 5 THR Z 330 ILE Z 338 -1 O GLU Z 334 N TYR Z 323
SHEET 5 AA3 5 GLY Z 392 GLU Z 395 -1 O GLY Z 392 N ILE Z 338
SHEET 1 AA4 8 LEU Z 252 GLY Z 254 0
SHEET 2 AA4 8 ARG Z 265 VAL Z 273 1 O SER Z 266 N ILE Z 253
SHEET 3 AA4 8 VAL Z 285 THR Z 291 -1 O ASP Z 290 N ARG Z 272
SHEET 4 AA4 8 TYR Z 278 ASP Z 279 -1 N TYR Z 278 O PHE Z 286
SHEET 5 AA4 8 VAL Z 285 THR Z 291 -1 O PHE Z 286 N TYR Z 278
SHEET 6 AA4 8 GLY Z 294 ALA Z 300 -1 O CYS Z 298 N PHE Z 287
SHEET 7 AA4 8 THR Z 330 ILE Z 338 1 O ILE Z 331 N LYS Z 297
SHEET 8 AA4 8 GLY Z 392 GLU Z 395 -1 O GLY Z 392 N ILE Z 338
SHEET 1 AA5 2 TRP Z 345 LYS Z 348 0
SHEET 2 AA5 2 LEU Z 381 LYS Z 384 -1 O GLU Z 383 N VAL Z 346
SHEET 1 AA6 3 GLU Z 360 SER Z 361 0
SHEET 2 AA6 3 PHE Z 368 CYS Z 370 -1 O ARG Z 369 N GLU Z 360
SHEET 3 AA6 3 THR Z 375 ALA Z 377 -1 O ALA Z 377 N PHE Z 368
LINK OD2 ASP Z 8 MG MG Z 508 1555 1555 2.53
LINK OD2 ASP Z 11 MG MG Z 507 1555 1555 2.54
LINK C CYS Z 17 N TPO Z 18 1555 1555 1.33
LINK O1P TPO Z 18 MG MG Z 507 1555 1555 2.28
LINK O2P TPO Z 18 MG MG Z 507 1555 1555 2.95
LINK O2P TPO Z 18 MG MG Z 508 1555 1555 2.37
LINK C TPO Z 18 N THR Z 19 1555 1555 1.33
LINK O GLY Z 57 MG MG Z 508 1555 1555 2.67
LINK SG CYS Z 352 ZN ZN Z 501 1555 1555 2.57
LINK SG CYS Z 355 ZN ZN Z 501 1555 1555 2.60
LINK SG CYS Z 370 ZN ZN Z 501 1555 1555 2.38
LINK SG CYS Z 373 ZN ZN Z 501 1555 1555 2.66
LINK O1B ACP Z 502 MG MG Z 508 1555 1555 2.50
LINK O1A ACP Z 502 MG MG Z 507 1555 1555 2.48
LINK O2A ACP Z 502 MG MG Z 507 1555 1555 2.87
LINK O2A ACP Z 502 MG MG Z 508 1555 1555 2.85
CISPEP 1 THR Z 53 ARG Z 54 0 0.95
CISPEP 2 TYR Z 188 PRO Z 189 0 12.94
SITE 1 AC1 4 CYS Z 352 CYS Z 355 CYS Z 370 CYS Z 373
SITE 1 AC2 21 ASP Z 8 ASP Z 9 ASP Z 11 TPO Z 18
SITE 2 AC2 21 LEU Z 45 ASN Z 46 TYR Z 51 ARG Z 54
SITE 3 AC2 21 GLY Z 55 ASN Z 56 GLY Z 57 ALA Z 112
SITE 4 AC2 21 ASP Z 115 VAL Z 116 LEU Z 117 ARG Z 140
SITE 5 AC2 21 GLY Z 141 ILE Z 143 GLY Z 144 MG Z 507
SITE 6 AC2 21 MG Z 508
SITE 1 AC3 8 GLU Z 159 ASP Z 193 ASN Z 194 VAL Z 203
SITE 2 AC3 8 CYS Z 204 GLY Z 215 ARG Z 217 SER Z 399
SITE 1 AC4 1 ARG Z 268
SITE 1 AC5 4 ARG Z 41 GLY Z 150 ALA Z 151 NH4 Z 506
SITE 1 AC6 4 ALA Z 102 VAL Z 103 GLY Z 150 ACT Z 505
SITE 1 AC7 5 ASP Z 9 THR Z 10 ASP Z 11 TPO Z 18
SITE 2 AC7 5 ACP Z 502
SITE 1 AC8 6 ASP Z 8 ASP Z 9 TPO Z 18 GLY Z 57
SITE 2 AC8 6 ALA Z 58 ACP Z 502
CRYST1 69.786 69.786 210.822 90.00 90.00 90.00 P 41 21 2 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 0.014330 0.000000 0.000000 0.00000
SCALE2 0.000000 0.014330 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004743 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
