HEADER DNA BINDING PROTEIN 17-JUL-17 5WHG
TITLE VMS1 MITOCHONDRIAL LOCALIZATION CORE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: PROTEIN VMS1;
COMPND 3 CHAIN: A;
COMPND 4 SYNONYM: VCP/CDC48-ASSOCIATED MITOCHONDRIAL STRESS-RESPONSIVE PROTEIN
COMPND 5 1;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE (STRAIN ATCC 204508 /
SOURCE 3 S288C);
SOURCE 4 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 5 ORGANISM_TAXID: 559292;
SOURCE 6 STRAIN: ATCC 204508 / S288C;
SOURCE 7 GENE: VMS1, YDR049W;
SOURCE 8 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 9 EXPRESSION_SYSTEM_TAXID: 562
KEYWDS ROS SIGNALLING, OXIDATIVE STRESS, MITOCHONDRIAL QUALITY CONTROL, DNA
KEYWDS 2 BINDING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR E.K.FREDRICKSON,H.L.SCHUBERT,J.RUTTER,C.P.HILL
REVDAT 3 01-JAN-20 5WHG 1 REMARK
REVDAT 2 29-NOV-17 5WHG 1 JRNL
REVDAT 1 15-NOV-17 5WHG 0
JRNL AUTH J.R.NIELSON,E.K.FREDRICKSON,T.C.WALLER,O.Z.RENDON,
JRNL AUTH 2 H.L.SCHUBERT,Z.LIN,C.P.HILL,J.RUTTER
JRNL TITL STEROL OXIDATION MEDIATES STRESS-RESPONSIVE VMS1
JRNL TITL 2 TRANSLOCATION TO MITOCHONDRIA.
JRNL REF MOL. CELL V. 68 673 2017
JRNL REFN ISSN 1097-4164
JRNL PMID 29149595
JRNL DOI 10.1016/J.MOLCEL.2017.10.022
REMARK 2
REMARK 2 RESOLUTION. 2.70 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX 1.11.1_2575
REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN
REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,
REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,
REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,
REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON,
REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,
REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT
REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART
REMARK 3
REMARK 3 REFINEMENT TARGET : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.70
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 24.06
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9
REMARK 3 NUMBER OF REFLECTIONS : 10237
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.193
REMARK 3 R VALUE (WORKING SET) : 0.187
REMARK 3 FREE R VALUE : 0.245
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 10.250
REMARK 3 FREE R VALUE TEST SET COUNT : 1041
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 24.0629 - 6.4641 0.99 1198 133 0.2151 0.2753
REMARK 3 2 6.4641 - 5.1473 1.00 1188 140 0.2075 0.2758
REMARK 3 3 5.1473 - 4.5014 1.00 1191 134 0.1479 0.2019
REMARK 3 4 4.5014 - 4.0921 1.00 1238 140 0.1466 0.1911
REMARK 3 5 4.0921 - 3.8000 1.00 1200 144 0.1585 0.2040
REMARK 3 6 3.8000 - 3.5767 1.00 1202 144 0.1837 0.2439
REMARK 3 7 3.5767 - 3.3981 1.00 1198 136 0.1849 0.2641
REMARK 3 8 3.3981 - 3.2505 1.00 1212 138 0.2072 0.2807
REMARK 3 9 3.2505 - 3.1257 1.00 1181 133 0.2012 0.2628
REMARK 3 10 3.1257 - 3.0180 1.00 1188 140 0.1777 0.2257
REMARK 3 11 3.0180 - 2.9238 1.00 1234 128 0.1879 0.2709
REMARK 3 12 2.9238 - 2.8404 1.00 1207 132 0.2126 0.2690
REMARK 3 13 2.8404 - 2.7657 1.00 1182 134 0.2708 0.3314
REMARK 3 14 2.7657 - 2.6983 1.00 1200 144 0.3056 0.3589
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
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) : 0.360
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.710
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 88.91
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 106.4
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 : 0.008 1770
REMARK 3 ANGLE : 0.972 2378
REMARK 3 CHIRALITY : 0.049 264
REMARK 3 PLANARITY : 0.006 294
REMARK 3 DIHEDRAL : 13.175 1068
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 1
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: ALL
REMARK 3 ORIGIN FOR THE GROUP (A): 26.7007 17.3242 58.6358
REMARK 3 T TENSOR
REMARK 3 T11: 0.7968 T22: 0.5182
REMARK 3 T33: 0.7214 T12: 0.1991
REMARK 3 T13: 0.0109 T23: -0.0998
REMARK 3 L TENSOR
REMARK 3 L11: 2.2558 L22: 5.6072
REMARK 3 L33: 6.9590 L12: -1.5529
REMARK 3 L13: -0.1731 L23: -0.8464
REMARK 3 S TENSOR
REMARK 3 S11: -0.0352 S12: -0.2923 S13: 0.1191
REMARK 3 S21: 0.6443 S22: 0.3049 S23: -0.0146
REMARK 3 S31: -0.6603 S32: -0.0663 S33: -0.2648
REMARK 3
REMARK 3 NCS DETAILS
REMARK 3 NUMBER OF NCS GROUPS : NULL
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: REFINED AGAINST I+,SIGI+, I-, SIGI-
REMARK 4
REMARK 4 5WHG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-JUL-17.
REMARK 100 THE DEPOSITION ID IS D_1000229005.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 03-AUG-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 8.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SSRL
REMARK 200 BEAMLINE : BL11-1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97862
REMARK 200 MONOCHROMATOR : SI(III)
REMARK 200 OPTICS : RH COATED FLAT
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO
REMARK 200 DATA SCALING SOFTWARE : SCALEPACK
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 10237
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.700
REMARK 200 RESOLUTION RANGE LOW (A) : 40.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.6
REMARK 200 DATA REDUNDANCY : 10.30
REMARK 200 R MERGE (I) : 0.07000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 9.7000
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) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 66.0
REMARK 200 DATA REDUNDANCY IN SHELL : 9.30
REMARK 200 R MERGE FOR SHELL (I) : 0.76300
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: 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 (%): 38.08
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.99
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 22-24% PEG MME 2000, 100 MM TRIS PH
REMARK 280 8.5, AND 0.2 M TMAO, EVAPORATION, TEMPERATURE 286K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 32 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -Y,X-Y,Z+2/3
REMARK 290 3555 -X+Y,-X,Z+1/3
REMARK 290 4555 Y,X,-Z
REMARK 290 5555 X-Y,-Y,-Z+1/3
REMARK 290 6555 -X,-X+Y,-Z+2/3
REMARK 290
REMARK 290 WHERE NNN -> OPERATOR NUMBER
REMARK 290 MMM -> TRANSLATION VECTOR
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY
REMARK 290 RELATED MOLECULES.
REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 2 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 2 0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 102.92200
REMARK 290 SMTRY1 3 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 3 -0.866025 -0.500000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 51.46100
REMARK 290 SMTRY1 4 -0.500000 0.866025 0.000000 0.00000
REMARK 290 SMTRY2 4 0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 5 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 51.46100
REMARK 290 SMTRY1 6 -0.500000 -0.866025 0.000000 0.00000
REMARK 290 SMTRY2 6 -0.866025 0.500000 0.000000 0.00000
REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 102.92200
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 APPLY THE FOLLOWING TO CHAINS: A
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 A -3
REMARK 465 ALA A -2
REMARK 465 MSE A -1
REMARK 465 GLY A 0
REMARK 465 MSE A 1
REMARK 465 ASN A 2
REMARK 465 SER A 3
REMARK 465 GLN A 4
REMARK 465 LYS A 5
REMARK 465 ALA A 6
REMARK 465 SER A 7
REMARK 465 LYS A 8
REMARK 465 MSE A 9
REMARK 465 THR A 10
REMARK 465 GLY A 11
REMARK 465 SER A 12
REMARK 465 PHE A 68
REMARK 465 ASP A 69
REMARK 465 ASN A 70
REMARK 465 VAL A 71
REMARK 465 MSE A 72
REMARK 465 ARG A 73
REMARK 465 PHE A 81
REMARK 465 ASP A 82
REMARK 465 SER A 83
REMARK 465 ARG A 84
REMARK 465 ASN A 85
REMARK 465 GLU A 86
REMARK 465 GLN A 87
REMARK 465 LYS A 88
REMARK 465 ALA A 89
REMARK 465 LEU A 107
REMARK 465 ASP A 108
REMARK 465 ILE A 109
REMARK 465 LEU A 110
REMARK 465 SER A 111
REMARK 465 VAL A 112
REMARK 465 GLU A 113
REMARK 465 GLU A 114
REMARK 465 PHE A 115
REMARK 465 ASP A 116
REMARK 465 ALA A 117
REMARK 465 LEU A 118
REMARK 465 ILE A 119
REMARK 465 SER A 120
REMARK 465 LYS A 121
REMARK 465 GLU A 122
REMARK 465 HIS A 123
REMARK 465 GLY A 124
REMARK 465 ILE A 125
REMARK 465 LYS A 126
REMARK 465 SER A 127
REMARK 465 GLU A 128
REMARK 465 ASP A 129
REMARK 465 GLU A 130
REMARK 465 ASN A 131
REMARK 465 SER A 132
REMARK 465 GLY A 133
REMARK 465 GLY A 134
REMARK 465 GLU A 135
REMARK 465 GLN A 136
REMARK 465 THR A 137
REMARK 465 SER A 138
REMARK 465 SER A 139
REMARK 465 ASP A 140
REMARK 465 HIS A 141
REMARK 465 GLU A 142
REMARK 465 GLU A 143
REMARK 465 SER A 144
REMARK 465 GLU A 145
REMARK 465 GLU A 146
REMARK 465 ALA A 147
REMARK 465 SER A 148
REMARK 465 ASP A 149
REMARK 465 ARG A 150
REMARK 465 ASP A 151
REMARK 465 PRO A 152
REMARK 465 ASP A 153
REMARK 465 LEU A 154
REMARK 465 GLN A 155
REMARK 465 THR A 156
REMARK 465 ASN A 157
REMARK 465 ASN A 158
REMARK 465 TYR A 159
REMARK 465 MSE A 160
REMARK 465 GLU A 161
REMARK 465 THR A 162
REMARK 465 ILE A 163
REMARK 465 ILE A 164
REMARK 465 GLU A 165
REMARK 465 ASN A 166
REMARK 465 ASP A 167
REMARK 465 LEU A 168
REMARK 465 GLN A 169
REMARK 465 LYS A 170
REMARK 465 LEU A 171
REMARK 465 GLY A 172
REMARK 465 PHE A 173
REMARK 465 GLN A 174
REMARK 465 LYS A 175
REMARK 465 ASP A 176
REMARK 465 GLU A 177
REMARK 465 SER A 178
REMARK 465 ASP A 179
REMARK 465 ALA A 180
REMARK 465 ILE A 181
REMARK 465 SER A 182
REMARK 465 HIS A 183
REMARK 465 ILE A 184
REMARK 465 ASN A 185
REMARK 465 THR A 186
REMARK 465 GLN A 187
REMARK 465 LEU A 198
REMARK 465 GLN A 199
REMARK 465 LYS A 200
REMARK 465 ASN A 201
REMARK 465 GLU A 202
REMARK 465 VAL A 258
REMARK 465 LYS A 259
REMARK 465 GLY A 260
REMARK 465 ASN A 261
REMARK 465 ALA A 262
REMARK 465 HIS A 263
REMARK 465 LYS A 264
REMARK 465 LYS A 265
REMARK 465 ASP A 266
REMARK 465 THR A 287
REMARK 465 ARG A 288
REMARK 465 ARG A 289
REMARK 465 LYS A 290
REMARK 465 GLN A 291
REMARK 465 GLY A 292
REMARK 465 GLY A 293
REMARK 465 SER A 294
REMARK 465 GLN A 295
REMARK 465 SER A 296
REMARK 465 ALA A 297
REMARK 465 MSE A 298
REMARK 465 ASP A 299
REMARK 465 ASN A 300
REMARK 465 ALA A 301
REMARK 465 LYS A 302
REMARK 465 GLY A 303
REMARK 465 LYS A 304
REMARK 465 ALA A 305
REMARK 465 ASN A 306
REMARK 465 SER A 307
REMARK 465 ALA A 308
REMARK 465 GLY A 309
REMARK 465 SER A 310
REMARK 465 ALA A 311
REMARK 465 LEU A 312
REMARK 465 ARG A 313
REMARK 465 ARG A 314
REMARK 465 TYR A 315
REMARK 465 ASN A 316
REMARK 465 GLU A 317
REMARK 465 PRO A 398
REMARK 465 GLU A 399
REMARK 465 PRO A 400
REMARK 465 LEU A 401
REMARK 465 ALA A 402
REMARK 465 VAL A 403
REMARK 465 LYS A 404
REMARK 465 GLU A 405
REMARK 465 THR A 406
REMARK 465 VAL A 407
REMARK 465 GLN A 408
REMARK 465 LYS A 409
REMARK 465 LEU A 410
REMARK 465 GLU A 411
REMARK 465 VAL A 412
REMARK 465 SER A 413
REMARK 465 ASN A 414
REMARK 465 LYS A 415
REMARK 465 LYS A 416
REMARK 465 ASP A 417
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 A 22 39.83 -157.80
REMARK 500 TYR A 91 -18.45 -151.27
REMARK 500 SER A 195 -85.48 -174.62
REMARK 500 LEU A 256 -158.71 -130.05
REMARK 500 ASP A 356 91.78 -69.66
REMARK 500 THR A 358 -154.97 -119.64
REMARK 500 PRO A 371 27.14 -76.08
REMARK 500 ASN A 375 -133.54 -90.43
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 ZN A 501 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 74 SG
REMARK 620 2 CYS A 77 SG 88.2
REMARK 620 3 HIS A 90 NE2 108.3 88.0
REMARK 620 4 HIS A 96 ND1 110.7 141.1 115.5
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 A 501
DBREF 5WHG A 1 417 UNP Q04311 VMS1_YEAST 1 417
SEQADV 5WHG GLY A -3 UNP Q04311 EXPRESSION TAG
SEQADV 5WHG ALA A -2 UNP Q04311 EXPRESSION TAG
SEQADV 5WHG MSE A -1 UNP Q04311 EXPRESSION TAG
SEQADV 5WHG GLY A 0 UNP Q04311 EXPRESSION TAG
SEQADV 5WHG A UNP Q04311 SER 38 DELETION
SEQADV 5WHG A UNP Q04311 THR 39 DELETION
SEQADV 5WHG A UNP Q04311 LEU 40 DELETION
SEQADV 5WHG A UNP Q04311 ARG 41 DELETION
SEQADV 5WHG A UNP Q04311 GLU 42 DELETION
SEQADV 5WHG A UNP Q04311 VAL 43 DELETION
SEQADV 5WHG A UNP Q04311 GLU 44 DELETION
SEQADV 5WHG A UNP Q04311 VAL 45 DELETION
SEQADV 5WHG A UNP Q04311 GLU 46 DELETION
SEQADV 5WHG A UNP Q04311 LYS 47 DELETION
SEQADV 5WHG A UNP Q04311 THR 48 DELETION
SEQADV 5WHG A UNP Q04311 SER 49 DELETION
SEQADV 5WHG A UNP Q04311 ASP 50 DELETION
SEQADV 5WHG A UNP Q04311 ASN 51 DELETION
SEQADV 5WHG A UNP Q04311 ASP 52 DELETION
SEQADV 5WHG A UNP Q04311 ARG 53 DELETION
SEQADV 5WHG A UNP Q04311 ASN 54 DELETION
SEQADV 5WHG A UNP Q04311 LYS 55 DELETION
SEQADV 5WHG A UNP Q04311 GLU 56 DELETION
SEQADV 5WHG A UNP Q04311 SER 57 DELETION
SEQADV 5WHG A UNP Q04311 GLY 58 DELETION
SEQADV 5WHG A UNP Q04311 ASP 59 DELETION
SEQADV 5WHG A UNP Q04311 LEU 60 DELETION
SEQADV 5WHG A UNP Q04311 GLN 61 DELETION
SEQADV 5WHG A UNP Q04311 ILE 62 DELETION
SEQADV 5WHG A UNP Q04311 ALA 63 DELETION
SEQADV 5WHG A UNP Q04311 ARG 64 DELETION
SEQADV 5WHG A UNP Q04311 LYS 65 DELETION
SEQADV 5WHG A UNP Q04311 LYS 66 DELETION
SEQADV 5WHG A UNP Q04311 VAL 67 DELETION
SEQADV 5WHG A UNP Q04311 THR 68 DELETION
SEQADV 5WHG A UNP Q04311 SER 69 DELETION
SEQRES 1 A 389 GLY ALA MSE GLY MSE ASN SER GLN LYS ALA SER LYS MSE
SEQRES 2 A 389 THR GLY SER LEU LYS LYS ASN ASP LEU TYR ILE PHE ASP
SEQRES 3 A 389 LEU SER GLU GLN LEU LEU ASN SER LEU LYS LEU MSE SER
SEQRES 4 A 389 PHE ASP ASN VAL MSE ARG CYS SER VAL CYS GLN MSE SER
SEQRES 5 A 389 PHE ASP SER ARG ASN GLU GLN LYS ALA HIS TYR GLN THR
SEQRES 6 A 389 ASP TYR HIS LEU MSE ASN VAL LYS ARG ASN LEU ARG GLY
SEQRES 7 A 389 LEU ASP ILE LEU SER VAL GLU GLU PHE ASP ALA LEU ILE
SEQRES 8 A 389 SER LYS GLU HIS GLY ILE LYS SER GLU ASP GLU ASN SER
SEQRES 9 A 389 GLY GLY GLU GLN THR SER SER ASP HIS GLU GLU SER GLU
SEQRES 10 A 389 GLU ALA SER ASP ARG ASP PRO ASP LEU GLN THR ASN ASN
SEQRES 11 A 389 TYR MSE GLU THR ILE ILE GLU ASN ASP LEU GLN LYS LEU
SEQRES 12 A 389 GLY PHE GLN LYS ASP GLU SER ASP ALA ILE SER HIS ILE
SEQRES 13 A 389 ASN THR GLN SER PRO TYR ILE TYR PHE LYS SER LYS TYR
SEQRES 14 A 389 LEU GLN LYS ASN GLU VAL LEU ALA ILE TYR LYS SER LEU
SEQRES 15 A 389 PHE ASN LYS ARG SER LEU SER ASN PRO ASN GLU ALA LEU
SEQRES 16 A 389 THR PHE TRP ASN SER GLN GLU ASN PRO MSE ALA ILE SER
SEQRES 17 A 389 ALA LEU PHE MSE VAL GLY GLY GLY HIS PHE ALA GLY ALA
SEQRES 18 A 389 ILE VAL SER HIS GLN ARG LEU ASN VAL LYS GLY ASN ALA
SEQRES 19 A 389 HIS LYS LYS ASP GLU THR LEU ILE GLU GLN ALA VAL ASN
SEQRES 20 A 389 PHE LEU GLU HIS LYS THR PHE HIS ARG TYR THR THR ARG
SEQRES 21 A 389 ARG LYS GLN GLY GLY SER GLN SER ALA MSE ASP ASN ALA
SEQRES 22 A 389 LYS GLY LYS ALA ASN SER ALA GLY SER ALA LEU ARG ARG
SEQRES 23 A 389 TYR ASN GLU SER ALA LEU LYS THR ASP ILE GLN GLY VAL
SEQRES 24 A 389 LEU LYS ASP TRP GLU PRO TYR LEU SER LYS CYS ASP ASN
SEQRES 25 A 389 ILE PHE ILE ARG ALA ARG ASN VAL SER ASP LYS LYS ILE
SEQRES 26 A 389 PHE THR ASP ASN THR VAL LEU ASN LYS GLY ASP GLU ARG
SEQRES 27 A 389 ILE LYS SER PHE PRO PHE THR THR ASN ARG PRO THR VAL
SEQRES 28 A 389 LEU GLU LEU LYS LYS ALA TRP CYS GLU LEU SER TYR LEU
SEQRES 29 A 389 LYS ILE LEU PRO LYS PRO GLU PRO LEU ALA VAL LYS GLU
SEQRES 30 A 389 THR VAL GLN LYS LEU GLU VAL SER ASN LYS LYS ASP
MODRES 5WHG MSE A 34 MET MODIFIED RESIDUE
MODRES 5WHG MSE A 79 MET MODIFIED RESIDUE
MODRES 5WHG MSE A 98 MET MODIFIED RESIDUE
MODRES 5WHG MSE A 233 MET MODIFIED RESIDUE
MODRES 5WHG MSE A 240 MET MODIFIED RESIDUE
HET MSE A 34 8
HET MSE A 79 8
HET MSE A 98 8
HET MSE A 233 8
HET MSE A 240 8
HET ZN A 501 1
HETNAM MSE SELENOMETHIONINE
HETNAM ZN ZINC ION
FORMUL 1 MSE 5(C5 H11 N O2 SE)
FORMUL 2 ZN ZN 2+
FORMUL 3 HOH *29(H2 O)
HELIX 1 AA1 LYS A 14 TYR A 19 5 6
HELIX 2 AA2 SER A 24 LEU A 31 1 8
HELIX 3 AA3 THR A 93 ARG A 105 1 13
HELIX 4 AA4 SER A 209 PHE A 211 5 3
HELIX 5 AA5 ASN A 218 ASN A 227 1 10
HELIX 6 AA6 THR A 268 ALA A 273 1 6
HELIX 7 AA7 ALA A 319 TRP A 331 1 13
HELIX 8 AA8 TRP A 331 LYS A 337 1 7
HELIX 9 AA9 ASN A 347 LYS A 352 1 6
HELIX 10 AB1 ILE A 353 THR A 355 5 3
HELIX 11 AB2 THR A 378 TYR A 391 1 14
SHEET 1 AA1 4 LYS A 32 LEU A 33 0
SHEET 2 AA1 4 TYR A 190 LYS A 194 -1 O LYS A 194 N LYS A 32
SHEET 3 AA1 4 LEU A 204 TYR A 207 -1 O LEU A 204 N PHE A 193
SHEET 4 AA1 4 LYS A 393 ILE A 394 -1 O LYS A 393 N ALA A 205
SHEET 1 AA2 5 ASN A 275 HIS A 283 0
SHEET 2 AA2 5 HIS A 245 SER A 252 -1 N SER A 252 O ASN A 275
SHEET 3 AA2 5 ILE A 235 GLY A 242 -1 N SER A 236 O VAL A 251
SHEET 4 AA2 5 ILE A 341 ARG A 344 1 O PHE A 342 N PHE A 239
SHEET 5 AA2 5 ILE A 367 LYS A 368 1 O LYS A 368 N ILE A 341
LINK C LEU A 33 N MSE A 34 1555 1555 1.33
LINK C MSE A 34 N SER A 35 1555 1555 1.33
LINK SG CYS A 74 ZN ZN A 501 1555 1555 2.41
LINK SG CYS A 77 ZN ZN A 501 1555 1555 2.33
LINK C GLN A 78 N MSE A 79 1555 1555 1.34
LINK C MSE A 79 N SER A 80 1555 1555 1.33
LINK NE2 HIS A 90 ZN ZN A 501 1555 1555 2.60
LINK ND1 HIS A 96 ZN ZN A 501 1555 1555 1.89
LINK C LEU A 97 N MSE A 98 1555 1555 1.33
LINK C MSE A 98 N ASN A 99 1555 1555 1.33
LINK C PRO A 232 N MSE A 233 1555 1555 1.33
LINK C MSE A 233 N ALA A 234 1555 1555 1.33
LINK C PHE A 239 N MSE A 240 1555 1555 1.33
LINK C MSE A 240 N VAL A 241 1555 1555 1.33
SITE 1 AC1 4 CYS A 74 CYS A 77 HIS A 90 HIS A 96
CRYST1 62.864 62.864 154.383 90.00 90.00 120.00 P 32 2 1 6
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 0.015907 0.009184 0.000000 0.00000
SCALE2 0.000000 0.018368 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006477 0.00000
(ATOM LINES ARE NOT SHOWN.)
END