HEADER HYDROLASE 29-MAR-12 4EFA
TITLE CRYSTAL STRUCTURE OF THE HETEROTRIMERIC EGCHEAD PERIPHERAL STALK
TITLE 2 COMPLEX OF THE YEAST VACUOLAR ATPASE - SECOND CONFORMATION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: V-TYPE PROTON ATPASE SUBUNIT C;
COMPND 3 CHAIN: C;
COMPND 4 FRAGMENT: UNP RESIDUES 158-277;
COMPND 5 SYNONYM: V-ATPASE SUBUNIT C, V-ATPASE 42 KDA SUBUNIT, VACUOLAR PROTON
COMPND 6 PUMP SUBUNIT C;
COMPND 7 EC: 3.6.3.14;
COMPND 8 ENGINEERED: YES;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: V-TYPE PROTON ATPASE SUBUNIT G;
COMPND 11 CHAIN: G;
COMPND 12 SYNONYM: V-ATPASE SUBUNIT G, V-ATPASE 13 KDA SUBUNIT, VACUOLAR PROTON
COMPND 13 PUMP SUBUNIT G;
COMPND 14 EC: 3.6.3.14;
COMPND 15 ENGINEERED: YES;
COMPND 16 MOL_ID: 3;
COMPND 17 MOLECULE: V-TYPE PROTON ATPASE SUBUNIT E;
COMPND 18 CHAIN: E;
COMPND 19 SYNONYM: V-ATPASE SUBUNIT E, V-ATPASE 27 KDA SUBUNIT, VACUOLAR PROTON
COMPND 20 PUMP SUBUNIT E;
COMPND 21 EC: 3.6.3.14;
COMPND 22 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 3 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 4 ORGANISM_TAXID: 559292;
SOURCE 5 STRAIN: ATCC 204508 / S288C;
SOURCE 6 GENE: VAT3, VATC, VMA5, YKL080W, YKL410;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: ROSETTA2;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PMALC2E;
SOURCE 12 MOL_ID: 2;
SOURCE 13 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 14 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 15 ORGANISM_TAXID: 559292;
SOURCE 16 STRAIN: ATCC 204508 / S288C;
SOURCE 17 GENE: VMA10, YHR039BC, YHR039C-A, YHR039C-B;
SOURCE 18 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 19 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 20 EXPRESSION_SYSTEM_STRAIN: ROSETTA2;
SOURCE 21 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 22 EXPRESSION_SYSTEM_PLASMID: PMALC2E;
SOURCE 23 MOL_ID: 3;
SOURCE 24 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 25 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 26 ORGANISM_TAXID: 559292;
SOURCE 27 STRAIN: ATCC 204508 / S288C;
SOURCE 28 GENE: O6241, VAT5, VMA4, YOR332W;
SOURCE 29 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 30 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 31 EXPRESSION_SYSTEM_STRAIN: ROSETTA2;
SOURCE 32 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 33 EXPRESSION_SYSTEM_PLASMID: PMALC2E
KEYWDS HETEROTRIMER, PERIPHERAL STALK, VACUOLAR ATPASE, HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR R.A.OOT,L.S.HUANG,E.A.BERRY,S.WILKENS
REVDAT 4 13-SEP-23 4EFA 1 REMARK SEQADV
REVDAT 3 15-NOV-17 4EFA 1 REMARK
REVDAT 2 28-NOV-12 4EFA 1 JRNL
REVDAT 1 10-OCT-12 4EFA 0
JRNL AUTH R.A.OOT,L.S.HUANG,E.A.BERRY,S.WILKENS
JRNL TITL CRYSTAL STRUCTURE OF THE YEAST VACUOLAR ATPASE
JRNL TITL 2 HETEROTRIMERIC EGC(HEAD) PERIPHERAL STALK COMPLEX.
JRNL REF STRUCTURE V. 20 1881 2012
JRNL REFN ISSN 0969-2126
JRNL PMID 23000382
JRNL DOI 10.1016/J.STR.2012.08.020
REMARK 2
REMARK 2 RESOLUTION. 2.82 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX DEV_1012
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : ML
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.82
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.66
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.3
REMARK 3 NUMBER OF REFLECTIONS : 14187
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.235
REMARK 3 R VALUE (WORKING SET) : 0.230
REMARK 3 FREE R VALUE : 0.277
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1418
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS).
REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE
REMARK 3 1 38.6587 - 6.0605 0.99 1374 153 0.2060 0.2473
REMARK 3 2 6.0605 - 4.8133 1.00 1312 146 0.2168 0.2527
REMARK 3 3 4.8133 - 4.2057 1.00 1293 144 0.1829 0.2367
REMARK 3 4 4.2057 - 3.8216 0.99 1273 140 0.2223 0.2897
REMARK 3 5 3.8216 - 3.5479 0.99 1255 139 0.2341 0.2799
REMARK 3 6 3.5479 - 3.3388 1.00 1257 140 0.2665 0.2964
REMARK 3 7 3.3388 - 3.1717 1.00 1276 141 0.2755 0.3397
REMARK 3 8 3.1717 - 3.0337 1.00 1240 138 0.2942 0.3592
REMARK 3 9 3.0337 - 2.9169 1.00 1280 142 0.2997 0.3434
REMARK 3 10 2.9169 - 2.8163 0.97 1209 135 0.3358 0.3715
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 1.00
REMARK 3 SHRINKAGE RADIUS : 0.73
REMARK 3 K_SOL : 0.33
REMARK 3 B_SOL : 58.29
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.380
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.190
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 93.53
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -6.39560
REMARK 3 B22 (A**2) : 1.48840
REMARK 3 B33 (A**2) : 4.90710
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 : 0.002 3433
REMARK 3 ANGLE : 0.499 4606
REMARK 3 CHIRALITY : 0.035 535
REMARK 3 PLANARITY : 0.002 588
REMARK 3 DIHEDRAL : 7.851 1353
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 9
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 158:172 )
REMARK 3 ORIGIN FOR THE GROUP (A):-107.0730 112.0629 156.9290
REMARK 3 T TENSOR
REMARK 3 T11: 0.3554 T22: 0.8351
REMARK 3 T33: 0.5409 T12: -0.1373
REMARK 3 T13: 0.0647 T23: -0.2151
REMARK 3 L TENSOR
REMARK 3 L11: 5.6385 L22: 6.2730
REMARK 3 L33: 2.2264 L12: -0.0814
REMARK 3 L13: 0.1737 L23: 2.9575
REMARK 3 S TENSOR
REMARK 3 S11: 0.0731 S12: 0.0776 S13: 0.8719
REMARK 3 S21: -0.5809 S22: 0.4371 S23: -0.3993
REMARK 3 S31: -0.5403 S32: 0.7007 S33: -0.5151
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 173:222 )
REMARK 3 ORIGIN FOR THE GROUP (A): -94.3856 93.1442 158.5256
REMARK 3 T TENSOR
REMARK 3 T11: 0.4371 T22: 0.6996
REMARK 3 T33: 0.3726 T12: 0.0171
REMARK 3 T13: 0.0006 T23: -0.1608
REMARK 3 L TENSOR
REMARK 3 L11: 4.1943 L22: 5.6774
REMARK 3 L33: 2.3424 L12: -1.3203
REMARK 3 L13: -2.1885 L23: 0.7618
REMARK 3 S TENSOR
REMARK 3 S11: 0.4795 S12: 0.2443 S13: -0.1795
REMARK 3 S21: -0.4895 S22: -0.2378 S23: -0.3886
REMARK 3 S31: 0.0522 S32: 0.4799 S33: -0.2159
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 223:230 )
REMARK 3 ORIGIN FOR THE GROUP (A): -97.0799 103.9559 161.5372
REMARK 3 T TENSOR
REMARK 3 T11: 0.4800 T22: 0.2648
REMARK 3 T33: 0.2761 T12: -0.1973
REMARK 3 T13: 0.0825 T23: -0.0602
REMARK 3 L TENSOR
REMARK 3 L11: 3.5113 L22: 3.7836
REMARK 3 L33: 9.5146 L12: -0.6646
REMARK 3 L13: -2.3911 L23: 2.2417
REMARK 3 S TENSOR
REMARK 3 S11: 0.3839 S12: -0.1022 S13: 0.0981
REMARK 3 S21: 0.2713 S22: 0.5024 S23: -0.1802
REMARK 3 S31: -0.1287 S32: 0.3088 S33: 0.6211
REMARK 3 TLS GROUP : 4
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 231:258 )
REMARK 3 ORIGIN FOR THE GROUP (A): -97.3643 88.4772 162.8563
REMARK 3 T TENSOR
REMARK 3 T11: 0.2122 T22: 0.4095
REMARK 3 T33: 0.2632 T12: -0.0206
REMARK 3 T13: -0.0717 T23: -0.0433
REMARK 3 L TENSOR
REMARK 3 L11: 7.7832 L22: 9.1847
REMARK 3 L33: 7.3755 L12: -1.1011
REMARK 3 L13: -2.2876 L23: 2.3443
REMARK 3 S TENSOR
REMARK 3 S11: 0.0717 S12: -0.1257 S13: -0.5600
REMARK 3 S21: 0.2541 S22: 0.2879 S23: -0.5989
REMARK 3 S31: 0.3400 S32: 0.4446 S33: -0.2439
REMARK 3 TLS GROUP : 5
REMARK 3 SELECTION: CHAIN 'C' AND (RESID 259:263 )
REMARK 3 ORIGIN FOR THE GROUP (A):-103.4058 90.2892 151.7954
REMARK 3 T TENSOR
REMARK 3 T11: 0.5827 T22: 1.1500
REMARK 3 T33: 0.8406 T12: -0.1489
REMARK 3 T13: -0.4127 T23: -0.0937
REMARK 3 L TENSOR
REMARK 3 L11: 7.5533 L22: 7.4716
REMARK 3 L33: 2.0001 L12: 0.4285
REMARK 3 L13: -1.7282 L23: -2.3388
REMARK 3 S TENSOR
REMARK 3 S11: 0.1042 S12: 1.5409 S13: -0.4933
REMARK 3 S21: -0.9538 S22: 0.1075 S23: 0.8413
REMARK 3 S31: 0.9183 S32: -0.4280 S33: -0.6601
REMARK 3 TLS GROUP : 6
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 2:60 )
REMARK 3 ORIGIN FOR THE GROUP (A): -84.1601 58.6900 131.2477
REMARK 3 T TENSOR
REMARK 3 T11: 0.4539 T22: 0.7731
REMARK 3 T33: 0.5782 T12: -0.0241
REMARK 3 T13: 0.0369 T23: -0.2115
REMARK 3 L TENSOR
REMARK 3 L11: 1.0615 L22: 5.2892
REMARK 3 L33: 8.2400 L12: 0.0220
REMARK 3 L13: 0.2709 L23: 6.6030
REMARK 3 S TENSOR
REMARK 3 S11: 0.1349 S12: -0.1573 S13: -0.1098
REMARK 3 S21: -0.8182 S22: 0.2542 S23: -0.7028
REMARK 3 S31: -0.3325 S32: 0.5039 S33: -0.2340
REMARK 3 TLS GROUP : 7
REMARK 3 SELECTION: CHAIN 'G' AND (RESID 61:105 )
REMARK 3 ORIGIN FOR THE GROUP (A): -83.2142 -17.0127 100.5418
REMARK 3 T TENSOR
REMARK 3 T11: 0.7908 T22: 0.9980
REMARK 3 T33: 1.0301 T12: 0.3043
REMARK 3 T13: -0.3607 T23: -0.2211
REMARK 3 L TENSOR
REMARK 3 L11: 0.1105 L22: 0.5885
REMARK 3 L33: 1.9453 L12: 0.0637
REMARK 3 L13: -0.0657 L23: -1.0670
REMARK 3 S TENSOR
REMARK 3 S11: -0.0095 S12: 0.2170 S13: 0.0675
REMARK 3 S21: 0.5201 S22: 0.8007 S23: -0.6018
REMARK 3 S31: 0.8498 S32: 1.5896 S33: -0.8549
REMARK 3 TLS GROUP : 8
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 2:111 )
REMARK 3 ORIGIN FOR THE GROUP (A): -87.1315 36.4746 125.9122
REMARK 3 T TENSOR
REMARK 3 T11: 0.9287 T22: 0.8053
REMARK 3 T33: 0.5954 T12: 0.1679
REMARK 3 T13: -0.2771 T23: -0.1941
REMARK 3 L TENSOR
REMARK 3 L11: 0.5045 L22: 4.6746
REMARK 3 L33: 2.8341 L12: 0.0336
REMARK 3 L13: -0.0457 L23: 3.6814
REMARK 3 S TENSOR
REMARK 3 S11: 0.1862 S12: 0.1253 S13: -0.2027
REMARK 3 S21: 1.5945 S22: 0.2772 S23: -0.3842
REMARK 3 S31: 1.2303 S32: 0.2963 S33: -0.4395
REMARK 3 TLS GROUP : 9
REMARK 3 SELECTION: CHAIN 'E' AND (RESID 112:226 )
REMARK 3 ORIGIN FOR THE GROUP (A): -96.1882 -28.5888 75.1828
REMARK 3 T TENSOR
REMARK 3 T11: 0.9400 T22: 0.7459
REMARK 3 T33: 0.7934 T12: 0.3108
REMARK 3 T13: -0.1676 T23: -0.2184
REMARK 3 L TENSOR
REMARK 3 L11: 2.1327 L22: 1.2121
REMARK 3 L33: 3.4620 L12: 1.3832
REMARK 3 L13: -0.0134 L23: -0.8981
REMARK 3 S TENSOR
REMARK 3 S11: 0.0404 S12: 0.7469 S13: -0.3634
REMARK 3 S21: -0.2145 S22: 0.5276 S23: -0.5372
REMARK 3 S31: 0.7745 S32: 0.4626 S33: -0.5575
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 4EFA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 02-APR-12.
REMARK 100 THE DEPOSITION ID IS D_1000071544.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-OCT-11
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : CHESS
REMARK 200 BEAMLINE : F1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.918
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : ADSC QUANTUM 270
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 14187
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 200 DATA REDUNDANCY : 13.90
REMARK 200 R MERGE (I) : 0.13200
REMARK 200 R SYM (I) : 0.13200
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 35.0890
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.85
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 14.10
REMARK 200 R MERGE FOR SHELL (I) : 0.00000
REMARK 200 R SYM FOR SHELL (I) : 0.00000
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.306
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER 2.5.0
REMARK 200 STARTING MODEL: PDB ENTRY 4DL0
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 52.63
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.60
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M LITHIUM SULFATE, 0.1 M MES, 20%
REMARK 280 PEG MME 2000, 0.15 M GLYCINE , PH 6, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 292K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 2 21 21
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+1/2,-Z+1/2
REMARK 290 4555 -X,-Y+1/2,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 0.00000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 46.82400
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 58.44550
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 46.82400
REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 58.44550
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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 7370 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 27150 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -113.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, G, E
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 GLY C 148
REMARK 465 PRO C 149
REMARK 465 LYS C 150
REMARK 465 VAL C 151
REMARK 465 PRO C 152
REMARK 465 GLU C 153
REMARK 465 SER C 154
REMARK 465 GLY C 155
REMARK 465 SER C 156
REMARK 465 MET C 157
REMARK 465 GLU C 264
REMARK 465 GLU C 265
REMARK 465 LEU C 266
REMARK 465 ILE C 267
REMARK 465 ASP C 268
REMARK 465 GLN C 269
REMARK 465 LEU C 270
REMARK 465 LYS C 271
REMARK 465 LYS C 272
REMARK 465 GLU C 273
REMARK 465 HIS C 274
REMARK 465 ASP C 275
REMARK 465 SER C 276
REMARK 465 ALA C 277
REMARK 465 GLY G -4
REMARK 465 PRO G -3
REMARK 465 LYS G -2
REMARK 465 VAL G -1
REMARK 465 PRO G 0
REMARK 465 MET G 1
REMARK 465 ALA G 62
REMARK 465 GLY G 63
REMARK 465 GLY G 64
REMARK 465 VAL G 65
REMARK 465 GLY G 66
REMARK 465 GLU G 67
REMARK 465 LEU G 68
REMARK 465 GLU G 69
REMARK 465 LYS G 70
REMARK 465 SER G 106
REMARK 465 ALA G 107
REMARK 465 GLU G 108
REMARK 465 VAL G 109
REMARK 465 HIS G 110
REMARK 465 ILE G 111
REMARK 465 ASN G 112
REMARK 465 ALA G 113
REMARK 465 LEU G 114
REMARK 465 MET E 1
REMARK 465 LYS E 227
REMARK 465 THR E 228
REMARK 465 ARG E 229
REMARK 465 LYS E 230
REMARK 465 PHE E 231
REMARK 465 PHE E 232
REMARK 465 ASP E 233
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 C 187 73.79 54.23
REMARK 500 SER C 209 -11.34 -142.75
REMARK 500 ASP C 228 -155.20 -116.72
REMARK 500 VAL G 76 -32.09 -131.38
REMARK 500 ASN E 112 40.75 -97.24
REMARK 500 MET E 152 27.59 -140.48
REMARK 500 ALA E 167 88.56 -154.46
REMARK 500 GLU E 170 -71.65 -85.66
REMARK 500 LEU E 220 31.21 -93.99
REMARK 500 GLU E 221 -41.28 -130.11
REMARK 500 TYR E 223 -153.36 -129.50
REMARK 500
REMARK 500 REMARK: NULL
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 301
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 G 201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 G 202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 G 203
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4DL0 RELATED DB: PDB
REMARK 900 SAME PROTEIN COMPLEX, DIFFERENT CONFORMATION
DBREF 4EFA C 158 277 UNP P31412 VATC_YEAST 158 277
DBREF 4EFA G 1 114 UNP P48836 VATG_YEAST 1 114
DBREF 4EFA E 1 233 UNP P22203 VATE_YEAST 1 233
SEQADV 4EFA GLY C 148 UNP P31412 EXPRESSION TAG
SEQADV 4EFA PRO C 149 UNP P31412 EXPRESSION TAG
SEQADV 4EFA LYS C 150 UNP P31412 EXPRESSION TAG
SEQADV 4EFA VAL C 151 UNP P31412 EXPRESSION TAG
SEQADV 4EFA PRO C 152 UNP P31412 EXPRESSION TAG
SEQADV 4EFA GLU C 153 UNP P31412 EXPRESSION TAG
SEQADV 4EFA SER C 154 UNP P31412 EXPRESSION TAG
SEQADV 4EFA GLY C 155 UNP P31412 EXPRESSION TAG
SEQADV 4EFA SER C 156 UNP P31412 EXPRESSION TAG
SEQADV 4EFA MET C 157 UNP P31412 EXPRESSION TAG
SEQADV 4EFA GLY G -4 UNP P48836 EXPRESSION TAG
SEQADV 4EFA PRO G -3 UNP P48836 EXPRESSION TAG
SEQADV 4EFA LYS G -2 UNP P48836 EXPRESSION TAG
SEQADV 4EFA VAL G -1 UNP P48836 EXPRESSION TAG
SEQADV 4EFA PRO G 0 UNP P48836 EXPRESSION TAG
SEQRES 1 C 130 GLY PRO LYS VAL PRO GLU SER GLY SER MET ASN LEU ALA
SEQRES 2 C 130 ALA ALA GLU ARG LYS LYS THR GLY ASP LEU SER VAL ARG
SEQRES 3 C 130 SER LEU HIS ASP ILE VAL LYS PRO GLU ASP PHE VAL LEU
SEQRES 4 C 130 ASN SER GLU HIS LEU THR THR VAL LEU VAL ALA VAL PRO
SEQRES 5 C 130 LYS SER LEU LYS SER ASP PHE GLU LYS SER TYR GLU THR
SEQRES 6 C 130 LEU SER LYS ASN VAL VAL PRO ALA SER ALA SER VAL ILE
SEQRES 7 C 130 ALA GLU ASP ALA GLU TYR VAL LEU PHE ASN VAL HIS LEU
SEQRES 8 C 130 PHE LYS LYS ASN VAL GLN GLU PHE THR THR ALA ALA ARG
SEQRES 9 C 130 GLU LYS LYS PHE ILE PRO ARG GLU PHE ASN TYR SER GLU
SEQRES 10 C 130 GLU LEU ILE ASP GLN LEU LYS LYS GLU HIS ASP SER ALA
SEQRES 1 G 119 GLY PRO LYS VAL PRO MET SER GLN LYS ASN GLY ILE ALA
SEQRES 2 G 119 THR LEU LEU GLN ALA GLU LYS GLU ALA HIS GLU ILE VAL
SEQRES 3 G 119 SER LYS ALA ARG LYS TYR ARG GLN ASP LYS LEU LYS GLN
SEQRES 4 G 119 ALA LYS THR ASP ALA ALA LYS GLU ILE ASP SER TYR LYS
SEQRES 5 G 119 ILE GLN LYS ASP LYS GLU LEU LYS GLU PHE GLU GLN LYS
SEQRES 6 G 119 ASN ALA GLY GLY VAL GLY GLU LEU GLU LYS LYS ALA GLU
SEQRES 7 G 119 ALA GLY VAL GLN GLY GLU LEU ALA GLU ILE LYS LYS ILE
SEQRES 8 G 119 ALA GLU LYS LYS LYS ASP ASP VAL VAL LYS ILE LEU ILE
SEQRES 9 G 119 GLU THR VAL ILE LYS PRO SER ALA GLU VAL HIS ILE ASN
SEQRES 10 G 119 ALA LEU
SEQRES 1 E 233 MET SER SER ALA ILE THR ALA LEU THR PRO ASN GLN VAL
SEQRES 2 E 233 ASN ASP GLU LEU ASN LYS MET GLN ALA PHE ILE ARG LYS
SEQRES 3 E 233 GLU ALA GLU GLU LYS ALA LYS GLU ILE GLN LEU LYS ALA
SEQRES 4 E 233 ASP GLN GLU TYR GLU ILE GLU LYS THR ASN ILE VAL ARG
SEQRES 5 E 233 ASN GLU THR ASN ASN ILE ASP GLY ASN PHE LYS SER LYS
SEQRES 6 E 233 LEU LYS LYS ALA MET LEU SER GLN GLN ILE THR LYS SER
SEQRES 7 E 233 THR ILE ALA ASN LYS MET ARG LEU LYS VAL LEU SER ALA
SEQRES 8 E 233 ARG GLU GLN SER LEU ASP GLY ILE PHE GLU GLU THR LYS
SEQRES 9 E 233 GLU LYS LEU SER GLY ILE ALA ASN ASN ARG ASP GLU TYR
SEQRES 10 E 233 LYS PRO ILE LEU GLN SER LEU ILE VAL GLU ALA LEU LEU
SEQRES 11 E 233 LYS LEU LEU GLU PRO LYS ALA ILE VAL LYS ALA LEU GLU
SEQRES 12 E 233 ARG ASP VAL ASP LEU ILE GLU SER MET LYS ASP ASP ILE
SEQRES 13 E 233 MET ARG GLU TYR GLY GLU LYS ALA GLN ARG ALA PRO LEU
SEQRES 14 E 233 GLU GLU ILE VAL ILE SER ASN ASP TYR LEU ASN LYS ASP
SEQRES 15 E 233 LEU VAL SER GLY GLY VAL VAL VAL SER ASN ALA SER ASP
SEQRES 16 E 233 LYS ILE GLU ILE ASN ASN THR LEU GLU GLU ARG LEU LYS
SEQRES 17 E 233 LEU LEU SER GLU GLU ALA LEU PRO ALA ILE ARG LEU GLU
SEQRES 18 E 233 LEU TYR GLY PRO SER LYS THR ARG LYS PHE PHE ASP
HET SO4 C 301 5
HET SO4 G 201 5
HET SO4 G 202 5
HET SO4 G 203 5
HETNAM SO4 SULFATE ION
FORMUL 4 SO4 4(O4 S 2-)
FORMUL 8 HOH *24(H2 O)
HELIX 1 1 LYS C 180 PHE C 184 5 5
HELIX 2 2 LEU C 202 LYS C 208 1 7
HELIX 3 3 SER C 209 LEU C 213 5 5
HELIX 4 4 ASN C 242 LYS C 253 1 12
HELIX 5 5 GLN G 3 ASN G 61 1 59
HELIX 6 6 VAL G 76 LYS G 90 1 15
HELIX 7 7 LYS G 90 ILE G 103 1 14
HELIX 8 8 THR E 9 ASN E 112 1 104
HELIX 9 9 ASN E 113 LEU E 133 1 21
HELIX 10 10 ASP E 145 GLU E 150 1 6
HELIX 11 11 MET E 152 ALA E 164 1 13
HELIX 12 12 LEU E 203 TYR E 223 1 21
SHEET 1 A 4 SER C 223 GLU C 227 0
SHEET 2 A 4 TYR C 231 PHE C 239 -1 O LEU C 233 N ILE C 225
SHEET 3 A 4 LEU C 191 PRO C 199 -1 N VAL C 196 O PHE C 234
SHEET 4 A 4 ILE C 256 ARG C 258 -1 O ILE C 256 N ALA C 197
SHEET 1 B 4 GLU E 171 ILE E 174 0
SHEET 2 B 4 LYS E 136 ALA E 141 1 N VAL E 139 O VAL E 173
SHEET 3 B 4 GLY E 187 SER E 191 -1 O SER E 191 N ILE E 138
SHEET 4 B 4 GLU E 198 THR E 202 -1 O ILE E 199 N VAL E 190
SITE 1 AC1 3 LEU C 175 ARG C 258 GLU C 259
SITE 1 AC2 1 ARG G 25
SITE 1 AC3 3 LYS E 31 ARG G 25 ARG G 28
SITE 1 AC4 3 HIS G 18 SER G 22 ARG G 25
CRYST1 51.537 93.648 116.891 90.00 90.00 90.00 P 2 21 21 4
ORIGX1 1.000000 0.000000 0.000000 0.00000
ORIGX2 0.000000 1.000000 0.000000 0.00000
ORIGX3 0.000000 0.000000 1.000000 0.00000
SCALE1 0.019404 0.000000 0.000000 0.00000
SCALE2 0.000000 0.010678 0.000000 0.00000
SCALE3 0.000000 0.000000 0.008555 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
