HEADER SIGNALING PROTEIN 05-MAR-15 4YLG
TITLE STRUCTURE OF AN ADP RIBOSYLATION FACTOR FROM ENTAMOEBA HISTOLYTICA HM-
TITLE 2 1:IMSS BOUND TO MG-GDP
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ADP-RIBOSYLATION FACTOR;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: SMALL GTPASE ARFA1;
COMPND 5 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: ENTAMOEBA HISTOLYTICA HM-1:IMSS;
SOURCE 3 ORGANISM_TAXID: 294381;
SOURCE 4 GENE: EHI_073470, EHI_137720;
SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS SIGNALING PROTEIN, STRUCTURAL GENOMICS, SEATTLE STRUCTURAL GENOMICS
KEYWDS 2 CENTER FOR INFECTIOUS DISEASE, SSGCID
EXPDTA X-RAY DIFFRACTION
AUTHOR SEATTLE STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE,SEATTLE
AUTHOR 2 STRUCTURAL GENOMICS CENTER FOR INFECTIOUS DISEASE (SSGCID)
REVDAT 2 27-SEP-23 4YLG 1 SOURCE REMARK LINK
REVDAT 1 20-MAY-15 4YLG 0
JRNL AUTH D.A.SERBZHINSKIY,M.C.CLIFTON,B.SANKARAN,B.L.STAKER,
JRNL AUTH 2 T.E.EDWARDS,P.J.MYLER
JRNL TITL STRUCTURE OF AN ADP-RIBOSYLATION FACTOR, ARF1, FROM
JRNL TITL 2 ENTAMOEBA HISTOLYTICA BOUND TO MG(2+)-GDP.
JRNL REF ACTA CRYSTALLOGR.,SECT.F V. 71 594 2015
JRNL REFN ESSN 2053-230X
JRNL PMID 25945714
JRNL DOI 10.1107/S2053230X15004677
REMARK 2
REMARK 2 RESOLUTION. 1.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX
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) : 1.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 19.73
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 93.4
REMARK 3 NUMBER OF REFLECTIONS : 34061
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.225
REMARK 3 R VALUE (WORKING SET) : 0.223
REMARK 3 FREE R VALUE : 0.272
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1702
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 19.7299 - 4.1094 0.99 2959 182 0.1582 0.1926
REMARK 3 2 4.1094 - 3.2665 0.96 2779 156 0.1665 0.2074
REMARK 3 3 3.2665 - 2.8550 0.99 2871 163 0.1841 0.2075
REMARK 3 4 2.8550 - 2.5946 0.97 2779 159 0.2022 0.2522
REMARK 3 5 2.5946 - 2.4090 0.99 2862 133 0.1996 0.2762
REMARK 3 6 2.4090 - 2.2672 0.93 2676 149 0.2417 0.3075
REMARK 3 7 2.2672 - 2.1538 0.88 2571 111 0.3342 0.4500
REMARK 3 8 2.1538 - 2.0601 0.91 2629 135 0.3196 0.3835
REMARK 3 9 2.0601 - 1.9809 0.93 2681 132 0.2699 0.3363
REMARK 3 10 1.9809 - 1.9126 0.85 2414 133 0.4194 0.4861
REMARK 3 11 1.9126 - 1.8528 0.82 2337 115 0.3738 0.4753
REMARK 3 12 1.8528 - 1.8000 0.97 2801 134 0.2320 0.3025
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) : 28.880
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 15.96
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 25.52
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 : 0.007 2649
REMARK 3 ANGLE : 1.140 3619
REMARK 3 CHIRALITY : 0.052 430
REMARK 3 PLANARITY : 0.004 445
REMARK 3 DIHEDRAL : 14.306 967
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 13
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 3 THROUGH 13 )
REMARK 3 ORIGIN FOR THE GROUP (A): 62.8532 11.3646 4.1695
REMARK 3 T TENSOR
REMARK 3 T11: 0.5105 T22: 0.5719
REMARK 3 T33: -0.0383 T12: -0.0863
REMARK 3 T13: 0.0935 T23: -0.0964
REMARK 3 L TENSOR
REMARK 3 L11: 0.1832 L22: 1.0038
REMARK 3 L33: 0.0589 L12: 0.0357
REMARK 3 L13: 0.0389 L23: -0.2117
REMARK 3 S TENSOR
REMARK 3 S11: -0.0136 S12: 0.0257 S13: 0.0454
REMARK 3 S21: -0.1572 S22: 0.0246 S23: -0.0400
REMARK 3 S31: -0.4022 S32: -0.1021 S33: -0.0398
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 14 THROUGH 33 )
REMARK 3 ORIGIN FOR THE GROUP (A): 53.2345 12.8716 18.5963
REMARK 3 T TENSOR
REMARK 3 T11: 0.1773 T22: 0.1356
REMARK 3 T33: 0.0388 T12: -0.0641
REMARK 3 T13: -0.0136 T23: 0.0367
REMARK 3 L TENSOR
REMARK 3 L11: 2.4259 L22: 2.1981
REMARK 3 L33: 2.6664 L12: -0.4976
REMARK 3 L13: -0.0571 L23: 0.8050
REMARK 3 S TENSOR
REMARK 3 S11: 0.0287 S12: 0.2985 S13: 0.0918
REMARK 3 S21: -0.0840 S22: 0.2147 S23: 0.0117
REMARK 3 S31: 0.0486 S32: 0.2119 S33: -0.1160
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 34 THROUGH 46 )
REMARK 3 ORIGIN FOR THE GROUP (A): 46.6138 4.6452 16.5346
REMARK 3 T TENSOR
REMARK 3 T11: 0.1162 T22: 0.1895
REMARK 3 T33: 0.0729 T12: -0.0228
REMARK 3 T13: 0.0024 T23: 0.0282
REMARK 3 L TENSOR
REMARK 3 L11: 3.4771 L22: 5.2030
REMARK 3 L33: 3.9631 L12: 0.5379
REMARK 3 L13: -0.6238 L23: -0.7067
REMARK 3 S TENSOR
REMARK 3 S11: -0.0841 S12: 0.0538 S13: -0.2416
REMARK 3 S21: -0.1169 S22: 0.0522 S23: 0.0764
REMARK 3 S31: 0.2591 S32: -0.0708 S33: 0.0318
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 47 THROUGH 63 )
REMARK 3 ORIGIN FOR THE GROUP (A): 52.9515 6.1737 15.1046
REMARK 3 T TENSOR
REMARK 3 T11: 0.1288 T22: 0.2808
REMARK 3 T33: 0.0453 T12: -0.0222
REMARK 3 T13: 0.0159 T23: 0.0288
REMARK 3 L TENSOR
REMARK 3 L11: 0.8418 L22: 1.9901
REMARK 3 L33: 4.1686 L12: -0.0923
REMARK 3 L13: -1.8306 L23: 0.5929
REMARK 3 S TENSOR
REMARK 3 S11: 0.0857 S12: 0.6418 S13: 0.1338
REMARK 3 S21: -0.1115 S22: 0.0723 S23: 0.1768
REMARK 3 S31: -0.0193 S32: -0.1525 S33: -0.1202
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 64 THROUGH 80 )
REMARK 3 ORIGIN FOR THE GROUP (A): 58.3230 0.7577 23.9914
REMARK 3 T TENSOR
REMARK 3 T11: 0.5313 T22: 0.2266
REMARK 3 T33: 0.3523 T12: -0.0344
REMARK 3 T13: 0.0153 T23: -0.0503
REMARK 3 L TENSOR
REMARK 3 L11: 3.2735 L22: 5.7017
REMARK 3 L33: 0.5584 L12: 1.1583
REMARK 3 L13: 0.6017 L23: -1.3263
REMARK 3 S TENSOR
REMARK 3 S11: -0.3662 S12: 0.3858 S13: -1.2373
REMARK 3 S21: 0.1636 S22: -0.3256 S23: 0.0742
REMARK 3 S31: 1.2699 S32: -0.4276 S33: 0.5804
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 81 THROUGH 92 )
REMARK 3 ORIGIN FOR THE GROUP (A): 58.6154 15.5761 24.2041
REMARK 3 T TENSOR
REMARK 3 T11: 0.1163 T22: 0.0485
REMARK 3 T33: 0.0209 T12: -0.0242
REMARK 3 T13: -0.0280 T23: 0.0185
REMARK 3 L TENSOR
REMARK 3 L11: 4.8875 L22: 4.6786
REMARK 3 L33: 4.8212 L12: -2.5814
REMARK 3 L13: -1.9342 L23: 1.8141
REMARK 3 S TENSOR
REMARK 3 S11: -0.1470 S12: 0.0674 S13: -0.0940
REMARK 3 S21: 0.2793 S22: 0.0919 S23: -0.0053
REMARK 3 S31: 0.0626 S32: 0.0214 S33: 0.0769
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 93 THROUGH 108 )
REMARK 3 ORIGIN FOR THE GROUP (A): 60.6818 13.0793 33.3352
REMARK 3 T TENSOR
REMARK 3 T11: 0.2590 T22: 0.1585
REMARK 3 T33: 0.0550 T12: -0.0381
REMARK 3 T13: -0.0622 T23: 0.0186
REMARK 3 L TENSOR
REMARK 3 L11: 2.5974 L22: 4.3070
REMARK 3 L33: 4.3145 L12: -1.4697
REMARK 3 L13: -1.1595 L23: 3.2994
REMARK 3 S TENSOR
REMARK 3 S11: -0.1646 S12: -0.0479 S13: -0.2738
REMARK 3 S21: 0.3788 S22: 0.2631 S23: -0.1771
REMARK 3 S31: 0.2773 S32: 0.0953 S33: -0.1009
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 109 THROUGH 122 )
REMARK 3 ORIGIN FOR THE GROUP (A): 65.6766 10.0099 21.6171
REMARK 3 T TENSOR
REMARK 3 T11: 0.1496 T22: 0.1743
REMARK 3 T33: 0.1321 T12: -0.0033
REMARK 3 T13: -0.0105 T23: -0.0262
REMARK 3 L TENSOR
REMARK 3 L11: 5.5418 L22: 4.4539
REMARK 3 L33: 5.0775 L12: -1.6823
REMARK 3 L13: -0.9691 L23: 1.2481
REMARK 3 S TENSOR
REMARK 3 S11: -0.0772 S12: 0.1740 S13: -0.5552
REMARK 3 S21: 0.1998 S22: -0.0110 S23: -0.2715
REMARK 3 S31: 0.4745 S32: 0.5800 S33: 0.0538
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 123 THROUGH 138 )
REMARK 3 ORIGIN FOR THE GROUP (A): 58.8293 27.0891 29.3006
REMARK 3 T TENSOR
REMARK 3 T11: 0.2179 T22: 0.0936
REMARK 3 T33: 0.2273 T12: -0.0206
REMARK 3 T13: -0.0386 T23: 0.0101
REMARK 3 L TENSOR
REMARK 3 L11: 3.0058 L22: 3.7047
REMARK 3 L33: 2.4456 L12: -2.7023
REMARK 3 L13: 2.0932 L23: -1.5024
REMARK 3 S TENSOR
REMARK 3 S11: -0.3489 S12: -0.1759 S13: 0.8003
REMARK 3 S21: 0.1083 S22: 0.1739 S23: -0.3373
REMARK 3 S31: -0.5165 S32: 0.0186 S33: 0.1598
REMARK 3 TLS GROUP : 10
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 139 THROUGH 161 )
REMARK 3 ORIGIN FOR THE GROUP (A): 64.9982 19.6240 22.2056
REMARK 3 T TENSOR
REMARK 3 T11: 0.1591 T22: 0.1201
REMARK 3 T33: 0.1474 T12: -0.0723
REMARK 3 T13: 0.0304 T23: -0.0093
REMARK 3 L TENSOR
REMARK 3 L11: 2.4573 L22: 1.8345
REMARK 3 L33: 3.1989 L12: 1.0131
REMARK 3 L13: -0.8365 L23: 1.1319
REMARK 3 S TENSOR
REMARK 3 S11: -0.0332 S12: 0.2441 S13: 0.1731
REMARK 3 S21: -0.2188 S22: 0.1529 S23: -0.3886
REMARK 3 S31: -0.2965 S32: 0.3928 S33: -0.0864
REMARK 3 TLS GROUP : 11
REMARK 3 SELECTION: CHAIN 'A' AND (RESID 162 THROUGH 173 )
REMARK 3 ORIGIN FOR THE GROUP (A): 65.1750 18.2541 12.3359
REMARK 3 T TENSOR
REMARK 3 T11: 0.3049 T22: 0.3151
REMARK 3 T33: 0.1334 T12: -0.0975
REMARK 3 T13: 0.0977 T23: -0.0060
REMARK 3 L TENSOR
REMARK 3 L11: 7.0495 L22: 3.8091
REMARK 3 L33: 3.3519 L12: -1.6104
REMARK 3 L13: -0.4918 L23: 0.0483
REMARK 3 S TENSOR
REMARK 3 S11: 0.2757 S12: 0.9105 S13: 0.4535
REMARK 3 S21: -0.8728 S22: -0.0461 S23: -0.4290
REMARK 3 S31: -0.3052 S32: 0.4299 S33: -0.1734
REMARK 3 TLS GROUP : 12
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 3 THROUGH 64 )
REMARK 3 ORIGIN FOR THE GROUP (A): 32.9836 5.1532 16.3391
REMARK 3 T TENSOR
REMARK 3 T11: 0.1347 T22: 0.2108
REMARK 3 T33: 0.1415 T12: -0.0369
REMARK 3 T13: -0.0148 T23: -0.0592
REMARK 3 L TENSOR
REMARK 3 L11: 2.2583 L22: 3.1951
REMARK 3 L33: 2.6858 L12: 0.0965
REMARK 3 L13: 0.0419 L23: -0.2580
REMARK 3 S TENSOR
REMARK 3 S11: -0.0809 S12: 0.5339 S13: -0.2332
REMARK 3 S21: -0.2733 S22: 0.0007 S23: 0.2965
REMARK 3 S31: 0.0635 S32: -0.1812 S33: 0.0058
REMARK 3 TLS GROUP : 13
REMARK 3 SELECTION: CHAIN 'B' AND (RESID 65 THROUGH 173 )
REMARK 3 ORIGIN FOR THE GROUP (A): 24.0431 5.1197 28.2981
REMARK 3 T TENSOR
REMARK 3 T11: 0.1226 T22: 0.0538
REMARK 3 T33: 0.1622 T12: -0.0205
REMARK 3 T13: 0.0217 T23: 0.0032
REMARK 3 L TENSOR
REMARK 3 L11: 2.4348 L22: 2.8878
REMARK 3 L33: 2.7967 L12: -0.2076
REMARK 3 L13: 0.0423 L23: 0.2219
REMARK 3 S TENSOR
REMARK 3 S11: 0.0031 S12: 0.2098 S13: 0.0031
REMARK 3 S21: 0.0087 S22: -0.0212 S23: 0.2933
REMARK 3 S31: -0.1307 S32: -0.1224 S33: 0.0383
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 4YLG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-MAR-15.
REMARK 100 THE DEPOSITION ID IS D_1000207654.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 18-OCT-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 7
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ALS
REMARK 200 BEAMLINE : 5.0.3
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : ASYMMETRIC CUT SINGLE CRYSTAL
REMARK 200 SI(220)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 315
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XSCALE
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34091
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.800
REMARK 200 RESOLUTION RANGE LOW (A) : 19.729
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 93.4
REMARK 200 DATA REDUNDANCY : 4.120
REMARK 200 R MERGE (I) : 0.06000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 15.9700
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 96.9
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : 0.43100
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 3.240
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: 1R8S
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 50.96
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.51
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% ETHANOL, 0.1M TRIS, CRYOPROTECTION
REMARK 280 25% ETHYLENE GLYCOL, PH 7.0, VAPOR DIFFUSION, SITTING DROP,
REMARK 280 TEMPERATURE 289K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
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+1/2,Y+1/2,Z
REMARK 290 4555 -X+1/2,Y+1/2,-Z
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 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 61.77000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 20.33000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 61.77000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 20.33000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON
REMARK 300 BURIED SURFACE AREA.
REMARK 350
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS
REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.
REMARK 350
REMARK 350 BIOMOLECULE: 1
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 3000 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 14860 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -47.0 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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH A 329 LIES ON A SPECIAL POSITION.
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 1
REMARK 465 GLY A 2
REMARK 465 GLN A 67
REMARK 465 ASP A 68
REMARK 465 LYS A 69
REMARK 465 ILE A 70
REMARK 465 ARG A 71
REMARK 465 PRO A 72
REMARK 465 MET B 1
REMARK 465 GLY B 2
REMARK 465 GLN B 67
REMARK 465 ASP B 68
REMARK 465 LYS B 69
REMARK 465 ILE B 70
REMARK 465 ARG B 71
REMARK 465 PRO B 72
REMARK 465 LEU B 73
REMARK 465 TRP B 74
REMARK 465 ARG B 75
REMARK 465 HIS B 76
REMARK 470
REMARK 470 MISSING ATOM
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 470 I=INSERTION CODE):
REMARK 470 M RES CSSEQI ATOMS
REMARK 470 LYS A 12 CG CD CE NZ
REMARK 470 GLU A 13 CG CD OE1 OE2
REMARK 470 GLU A 53 CG CD OE1 OE2
REMARK 470 ARG A 75 CG CD NE CZ NH1 NH2
REMARK 470 HIS A 76 CG ND1 CD2 CE1 NE2
REMARK 470 TYR A 77 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLN A 79 CG CD OE1 NE2
REMARK 470 GLU A 111 CG CD OE1 OE2
REMARK 470 LYS A 145 CG CD CE NZ
REMARK 470 TYR A 163 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LYS B 11 CG CD CE NZ
REMARK 470 LYS B 12 CG CD CE NZ
REMARK 470 GLU B 13 CG CD OE1 OE2
REMARK 470 GLU B 53 CG CD OE1 OE2
REMARK 470 LYS B 55 CG CD CE NZ
REMARK 470 TYR B 77 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 TYR B 78 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 GLN B 79 CG CD OE1 NE2
REMARK 470 ASN B 80 CG OD1 ND2
REMARK 470 GLU B 111 CG CD OE1 OE2
REMARK 470 LYS B 145 CG CD CE NZ
REMARK 470 LYS B 148 CG CD CE NZ
REMARK 470 TYR B 163 CG CD1 CD2 CE1 CE2 CZ OH
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 OE1 GLN B 82 O HOH B 440 2.16
REMARK 500 O HOH A 398 O HOH A 414 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 O HOH A 310 O HOH A 310 2655 2.11
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 LYS A 55 -117.44 50.81
REMARK 500 LYS B 55 -116.60 49.91
REMARK 500 ASP B 92 78.72 -112.99
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 B 416 DISTANCE = 5.84 ANGSTROMS
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG A 202 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR A 27 OG1
REMARK 620 2 GDP A 201 O1B 82.7
REMARK 620 3 HOH A 349 O 108.9 89.8
REMARK 620 4 HOH A 383 O 104.7 172.6 88.6
REMARK 620 5 HOH A 384 O 86.1 97.8 164.0 82.1
REMARK 620 6 HOH A 406 O 170.1 104.0 78.7 68.6 85.7
REMARK 620 N 1 2 3 4 5
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 MG B 202 MG
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 THR B 27 OG1
REMARK 620 2 GDP B 201 O1B 83.8
REMARK 620 3 HOH B 361 O 171.2 103.7
REMARK 620 4 HOH B 399 O 92.4 89.9 83.1
REMARK 620 5 HOH B 415 O 104.4 90.2 80.4 163.1
REMARK 620 6 HOH B 429 O 98.8 176.2 73.9 92.7 86.6
REMARK 620 N 1 2 3 4 5
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GDP A 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG A 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue GDP B 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue MG B 202
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: SSGCID-ENHIA.01533.A RELATED DB: TARGETTRACK
DBREF 4YLG A 1 173 UNP C4LXL1 C4LXL1_ENTHI 1 173
DBREF 4YLG B 1 173 UNP C4LXL1 C4LXL1_ENTHI 1 173
SEQRES 1 A 173 MET GLY SER TRP LEU SER LYS LEU LEU GLY LYS LYS GLU
SEQRES 2 A 173 MET ARG ILE LEU MET VAL GLY LEU ASP ALA ALA GLY LYS
SEQRES 3 A 173 THR SER ILE LEU TYR LYS LEU LYS LEU GLY GLU ILE VAL
SEQRES 4 A 173 THR THR ILE PRO THR ILE GLY PHE ASN VAL GLU THR VAL
SEQRES 5 A 173 GLU TYR LYS ASN ILE SER PHE THR VAL TRP ASP VAL GLY
SEQRES 6 A 173 GLY GLN ASP LYS ILE ARG PRO LEU TRP ARG HIS TYR TYR
SEQRES 7 A 173 GLN ASN THR GLN ALA ILE ILE PHE VAL VAL ASP SER ASN
SEQRES 8 A 173 ASP ARG ASP ARG ILE GLY GLU ALA ARG GLU GLU LEU MET
SEQRES 9 A 173 LYS MET LEU ASN GLU ASP GLU MET ARG ASN ALA ILE LEU
SEQRES 10 A 173 LEU VAL PHE ALA ASN LYS HIS ASP LEU PRO GLN ALA MET
SEQRES 11 A 173 SER ILE SER GLU VAL THR GLU LYS LEU GLY LEU GLN THR
SEQRES 12 A 173 ILE LYS ASN ARG LYS TRP TYR CYS GLN THR SER CYS ALA
SEQRES 13 A 173 THR ASN GLY ASP GLY LEU TYR GLU GLY LEU ASP TRP LEU
SEQRES 14 A 173 ALA ASP ASN LEU
SEQRES 1 B 173 MET GLY SER TRP LEU SER LYS LEU LEU GLY LYS LYS GLU
SEQRES 2 B 173 MET ARG ILE LEU MET VAL GLY LEU ASP ALA ALA GLY LYS
SEQRES 3 B 173 THR SER ILE LEU TYR LYS LEU LYS LEU GLY GLU ILE VAL
SEQRES 4 B 173 THR THR ILE PRO THR ILE GLY PHE ASN VAL GLU THR VAL
SEQRES 5 B 173 GLU TYR LYS ASN ILE SER PHE THR VAL TRP ASP VAL GLY
SEQRES 6 B 173 GLY GLN ASP LYS ILE ARG PRO LEU TRP ARG HIS TYR TYR
SEQRES 7 B 173 GLN ASN THR GLN ALA ILE ILE PHE VAL VAL ASP SER ASN
SEQRES 8 B 173 ASP ARG ASP ARG ILE GLY GLU ALA ARG GLU GLU LEU MET
SEQRES 9 B 173 LYS MET LEU ASN GLU ASP GLU MET ARG ASN ALA ILE LEU
SEQRES 10 B 173 LEU VAL PHE ALA ASN LYS HIS ASP LEU PRO GLN ALA MET
SEQRES 11 B 173 SER ILE SER GLU VAL THR GLU LYS LEU GLY LEU GLN THR
SEQRES 12 B 173 ILE LYS ASN ARG LYS TRP TYR CYS GLN THR SER CYS ALA
SEQRES 13 B 173 THR ASN GLY ASP GLY LEU TYR GLU GLY LEU ASP TRP LEU
SEQRES 14 B 173 ALA ASP ASN LEU
HET GDP A 201 28
HET MG A 202 1
HET GDP B 201 28
HET MG B 202 1
HETNAM GDP GUANOSINE-5'-DIPHOSPHATE
HETNAM MG MAGNESIUM ION
FORMUL 3 GDP 2(C10 H15 N5 O11 P2)
FORMUL 4 MG 2(MG 2+)
FORMUL 7 HOH *313(H2 O)
HELIX 1 AA1 SER A 3 LEU A 9 1 7
HELIX 2 AA2 GLY A 25 LYS A 34 1 10
HELIX 3 AA3 LEU A 73 GLN A 79 5 7
HELIX 4 AA4 ASP A 92 ASP A 94 5 3
HELIX 5 AA5 ARG A 95 ASN A 108 1 14
HELIX 6 AA6 GLU A 109 ARG A 113 5 5
HELIX 7 AA7 SER A 131 LEU A 139 1 9
HELIX 8 AA8 GLY A 140 ILE A 144 5 5
HELIX 9 AA9 GLY A 161 ASN A 172 1 12
HELIX 10 AB1 TRP B 4 LEU B 9 1 6
HELIX 11 AB2 GLY B 25 LYS B 34 1 10
HELIX 12 AB3 ARG B 95 ASN B 108 1 14
HELIX 13 AB4 GLU B 109 ARG B 113 5 5
HELIX 14 AB5 SER B 131 LEU B 139 1 9
HELIX 15 AB6 GLY B 140 ILE B 144 5 5
HELIX 16 AB7 GLY B 161 ASN B 172 1 12
SHEET 1 AA114 TRP A 149 THR A 153 0
SHEET 2 AA114 ILE A 116 ASN A 122 1 N VAL A 119 O GLN A 152
SHEET 3 AA114 THR A 81 ASP A 89 1 N ILE A 84 O LEU A 118
SHEET 4 AA114 MET A 14 GLY A 20 1 N LEU A 17 O ILE A 85
SHEET 5 AA114 ILE A 57 ASP A 63 1 O THR A 60 N MET A 18
SHEET 6 AA114 PHE A 47 TYR A 54 -1 N GLU A 50 O VAL A 61
SHEET 7 AA114 ILE A 38 THR A 44 -1 N THR A 41 O VAL A 49
SHEET 8 AA114 ILE B 38 THR B 44 -1 O ILE B 38 N THR A 40
SHEET 9 AA114 PHE B 47 TYR B 54 -1 O VAL B 49 N THR B 41
SHEET 10 AA114 ILE B 57 ASP B 63 -1 O ILE B 57 N TYR B 54
SHEET 11 AA114 MET B 14 GLY B 20 1 N ILE B 16 O SER B 58
SHEET 12 AA114 THR B 81 ASP B 89 1 O ILE B 85 N LEU B 17
SHEET 13 AA114 ILE B 116 ASN B 122 1 O LEU B 118 N ILE B 84
SHEET 14 AA114 TRP B 149 THR B 153 1 O TYR B 150 N VAL B 119
LINK OG1 THR A 27 MG MG A 202 1555 1555 2.11
LINK O1B GDP A 201 MG MG A 202 1555 1555 1.95
LINK MG MG A 202 O HOH A 349 1555 1555 2.25
LINK MG MG A 202 O HOH A 383 1555 1555 2.07
LINK MG MG A 202 O HOH A 384 1555 1555 2.18
LINK MG MG A 202 O HOH A 406 1555 1555 2.64
LINK OG1 THR B 27 MG MG B 202 1555 1555 2.20
LINK O1B GDP B 201 MG MG B 202 1555 1555 2.03
LINK MG MG B 202 O HOH B 361 1555 1555 2.55
LINK MG MG B 202 O HOH B 399 1555 1555 2.23
LINK MG MG B 202 O HOH B 415 1555 1555 1.97
LINK MG MG B 202 O HOH B 429 1555 1555 2.32
SITE 1 AC1 21 ALA A 23 ALA A 24 GLY A 25 LYS A 26
SITE 2 AC1 21 THR A 27 SER A 28 ASN A 122 LYS A 123
SITE 3 AC1 21 ASP A 125 CYS A 155 ALA A 156 MG A 202
SITE 4 AC1 21 HOH A 349 HOH A 362 HOH A 382 HOH A 384
SITE 5 AC1 21 HOH A 406 HOH A 442 HOH A 445 GLY B 46
SITE 6 AC1 21 ASN B 48
SITE 1 AC2 6 THR A 27 GDP A 201 HOH A 349 HOH A 383
SITE 2 AC2 6 HOH A 384 HOH A 406
SITE 1 AC3 23 ILE A 45 GLY A 46 ASN A 48 ALA B 23
SITE 2 AC3 23 ALA B 24 GLY B 25 LYS B 26 THR B 27
SITE 3 AC3 23 SER B 28 ASN B 122 LYS B 123 ASP B 125
SITE 4 AC3 23 LEU B 126 CYS B 155 ALA B 156 THR B 157
SITE 5 AC3 23 MG B 202 HOH B 361 HOH B 387 HOH B 399
SITE 6 AC3 23 HOH B 415 HOH B 443 HOH B 454
SITE 1 AC4 6 THR B 27 GDP B 201 HOH B 361 HOH B 399
SITE 2 AC4 6 HOH B 415 HOH B 429
CRYST1 123.540 40.660 78.950 90.00 97.45 90.00 C 1 2 1 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 0.008095 0.000000 0.001058 0.00000
SCALE2 0.000000 0.024594 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012774 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
