HEADER CELL CYCLE 13-NOV-14 4WX8
TITLE CRYSTAL STRUCTURE OF BINARY COMPLEX GON7-PCC1
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: EKC/KEOPS COMPLEX SUBUNIT PCC1;
COMPND 3 CHAIN: A, B, C;
COMPND 4 SYNONYM: POLARIZED GROWTH CHROMATIN-ASSOCIATED CONTROLLER 1;
COMPND 5 ENGINEERED: YES;
COMPND 6 MOL_ID: 2;
COMPND 7 MOLECULE: EKC/KEOPS COMPLEX SUBUNIT GON7;
COMPND 8 CHAIN: D, E, F;
COMPND 9 SYNONYM: LOW-DYE-BINDING PROTEIN 6,POLARIZED GROWTH CHROMATIN-
COMPND 10 ASSOCIATED CONTROLLER 2;
COMPND 11 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: PCC1, YKR095W-A;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI 'BL21-GOLD(DE3)PLYSS AG';
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 866768;
SOURCE 9 MOL_ID: 2;
SOURCE 10 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 11 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 12 ORGANISM_TAXID: 559292;
SOURCE 13 STRAIN: ATCC 204508 / S288C;
SOURCE 14 GENE: GON7, LDB6, PCC2, YJL184W, J0420;
SOURCE 15 EXPRESSION_SYSTEM: ESCHERICHIA COLI 'BL21-GOLD(DE3)PLYSS AG';
SOURCE 16 EXPRESSION_SYSTEM_TAXID: 866768
KEYWDS KEOPS, GON7-PCC1, TRNA T6A, CELL CYCLE
EXPDTA X-RAY DIFFRACTION
AUTHOR W.ZHANG,H.VAN TILBEURGH
REVDAT 3 26-AUG-15 4WX8 1
REVDAT 2 15-APR-15 4WX8 1 JRNL
REVDAT 1 18-MAR-15 4WX8 0
JRNL AUTH W.ZHANG,B.COLLINET,M.GRAILLE,M.C.DAUGERON,N.LAZAR,D.LIBRI,
JRNL AUTH 2 D.DURAND,H.VAN TILBEURGH
JRNL TITL CRYSTAL STRUCTURES OF THE GON7/PCC1 AND BUD32/CGI121
JRNL TITL 2 COMPLEXES PROVIDE A MODEL FOR THE COMPLETE YEAST KEOPS
JRNL TITL 3 COMPLEX.
JRNL REF NUCLEIC ACIDS RES. V. 43 3358 2015
JRNL REFN ESSN 1362-4962
JRNL PMID 25735745
JRNL DOI 10.1093/NAR/GKV155
REMARK 2
REMARK 2 RESOLUTION. 2.99 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0071
REMARK 3 AUTHORS : MURSHUDOV,VAGIN,DODSON
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.99
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 43.53
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 3 NUMBER OF REFLECTIONS : 12660
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.254
REMARK 3 R VALUE (WORKING SET) : 0.251
REMARK 3 FREE R VALUE : 0.308
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 667
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 2.99
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.07
REMARK 3 REFLECTION IN BIN (WORKING SET) : 936
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 96.66
REMARK 3 BIN R VALUE (WORKING SET) : 0.4000
REMARK 3 BIN FREE R VALUE SET COUNT : 49
REMARK 3 BIN FREE R VALUE : 0.4730
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 3060
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 4
REMARK 3 SOLVENT ATOMS : 14
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 66.14
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.43000
REMARK 3 B22 (A**2) : -0.44000
REMARK 3 B33 (A**2) : 1.57000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -1.51000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): 2.274
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.463
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.399
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 42.091
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.909
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.883
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 3103 ; 0.011 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 2839 ; 0.002 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 4226 ; 1.481 ; 1.987
REMARK 3 BOND ANGLES OTHERS (DEGREES): 6499 ; 0.678 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 412 ; 5.859 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 114 ;29.634 ;25.965
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 443 ;17.271 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 9 ;22.714 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 528 ; 0.069 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 3520 ; 0.019 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): 614 ; 0.016 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 1682 ; 2.581 ; 3.645
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 1680 ; 2.566 ; 3.642
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 2082 ; 4.134 ; 6.106
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 2083 ; 4.133 ; 6.108
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 1421 ; 3.482 ; 3.814
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 1422 ; 3.480 ; 3.815
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 2145 ; 4.746 ; 6.333
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): 3608 ; 5.608 ; 8.119
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): 3608 ; 5.608 ; 8.119
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : 2
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B C
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 7 A 90 4
REMARK 3 1 B 7 B 90 4
REMARK 3 1 C 7 C 90 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 979 ; 0.56 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 B (A): 979 ; 0.48 ; 0.50
REMARK 3 MEDIUM POSITIONAL 1 B (A): 979 ; 0.53 ; 0.50
REMARK 3 MEDIUM THERMAL 1 A (A**2): 979 ; 4.27 ; 5.00
REMARK 3 MEDIUM THERMAL 1 B (A**2): 979 ; 3.48 ; 5.00
REMARK 3 MEDIUM THERMAL 1 C (A**2): 979 ; 4.20 ; 5.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : D E
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 D 2 D 113 4
REMARK 3 1 E 2 E 113 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 2 D (A): 804 ; 0.40 ; 0.50
REMARK 3 MEDIUM THERMAL 2 D (A**2): 804 ; 3.49 ; 5.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 6
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 9 A 90
REMARK 3 ORIGIN FOR THE GROUP (A): -4.8280 68.6330 82.5980
REMARK 3 T TENSOR
REMARK 3 T11: 0.3584 T22: 0.4266
REMARK 3 T33: 0.1280 T12: 0.0648
REMARK 3 T13: 0.1373 T23: 0.0220
REMARK 3 L TENSOR
REMARK 3 L11: 2.2893 L22: 2.4155
REMARK 3 L33: 3.0657 L12: 0.7005
REMARK 3 L13: 0.9736 L23: 1.9724
REMARK 3 S TENSOR
REMARK 3 S11: -0.2970 S12: 0.0470 S13: 0.1092
REMARK 3 S21: -0.1716 S22: -0.0240 S23: 0.2458
REMARK 3 S31: -0.2925 S32: -0.3271 S33: 0.3210
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 8 B 90
REMARK 3 ORIGIN FOR THE GROUP (A): -8.2080 43.1880 66.4510
REMARK 3 T TENSOR
REMARK 3 T11: 0.3860 T22: 0.5307
REMARK 3 T33: 0.0621 T12: -0.1368
REMARK 3 T13: 0.1204 T23: -0.0326
REMARK 3 L TENSOR
REMARK 3 L11: 1.3993 L22: 2.4124
REMARK 3 L33: 2.3232 L12: -0.1592
REMARK 3 L13: -0.8300 L23: 0.0521
REMARK 3 S TENSOR
REMARK 3 S11: -0.1195 S12: 0.2002 S13: -0.1580
REMARK 3 S21: -0.2741 S22: 0.1128 S23: 0.0259
REMARK 3 S31: 0.2101 S32: -0.6787 S33: 0.0066
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 9 C 88
REMARK 3 ORIGIN FOR THE GROUP (A): 8.3250 53.6040 42.6690
REMARK 3 T TENSOR
REMARK 3 T11: 0.5880 T22: 0.5710
REMARK 3 T33: 0.1292 T12: -0.0528
REMARK 3 T13: 0.1733 T23: -0.0187
REMARK 3 L TENSOR
REMARK 3 L11: 3.9283 L22: 2.9877
REMARK 3 L33: 3.3914 L12: 1.2029
REMARK 3 L13: -0.0182 L23: -0.0215
REMARK 3 S TENSOR
REMARK 3 S11: -0.0096 S12: 0.6157 S13: -0.0175
REMARK 3 S21: -0.5488 S22: 0.0781 S23: 0.1664
REMARK 3 S31: 0.4514 S32: 0.0058 S33: -0.0685
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 3 D 111
REMARK 3 ORIGIN FOR THE GROUP (A): 22.8440 68.2110 68.2780
REMARK 3 T TENSOR
REMARK 3 T11: 0.4621 T22: 0.6774
REMARK 3 T33: 0.2970 T12: 0.0157
REMARK 3 T13: 0.2289 T23: 0.0458
REMARK 3 L TENSOR
REMARK 3 L11: 1.4496 L22: 2.7631
REMARK 3 L33: 3.2752 L12: -1.8826
REMARK 3 L13: 2.1103 L23: -2.6298
REMARK 3 S TENSOR
REMARK 3 S11: -0.1537 S12: 0.3177 S13: 0.3731
REMARK 3 S21: -0.0564 S22: -0.3464 S23: -0.7174
REMARK 3 S31: -0.1642 S32: 0.7429 S33: 0.5001
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 3 E 109
REMARK 3 ORIGIN FOR THE GROUP (A): -0.5480 34.8810 75.0610
REMARK 3 T TENSOR
REMARK 3 T11: 1.0349 T22: 0.5978
REMARK 3 T33: 0.2165 T12: -0.1044
REMARK 3 T13: 0.3235 T23: -0.0331
REMARK 3 L TENSOR
REMARK 3 L11: 0.4144 L22: 0.0519
REMARK 3 L33: 0.3028 L12: 0.1313
REMARK 3 L13: 0.1671 L23: 0.0063
REMARK 3 S TENSOR
REMARK 3 S11: -0.0733 S12: 0.0713 S13: -0.2339
REMARK 3 S21: -0.1214 S22: 0.0357 S23: -0.1013
REMARK 3 S31: 0.4580 S32: 0.0074 S33: 0.0376
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 3 F 94
REMARK 3 ORIGIN FOR THE GROUP (A): 15.2350 62.1770 49.3240
REMARK 3 T TENSOR
REMARK 3 T11: 0.5150 T22: 0.4663
REMARK 3 T33: 0.2941 T12: -0.0713
REMARK 3 T13: 0.1821 T23: 0.0799
REMARK 3 L TENSOR
REMARK 3 L11: 3.9911 L22: 3.8519
REMARK 3 L33: 4.0444 L12: -2.7018
REMARK 3 L13: 2.2973 L23: -1.7575
REMARK 3 S TENSOR
REMARK 3 S11: 0.1190 S12: 0.6337 S13: 0.7643
REMARK 3 S21: -0.2912 S22: -0.1369 S23: -0.2740
REMARK 3 S31: -0.0255 S32: 0.5821 S33: 0.0178
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS
REMARK 4
REMARK 4 4WX8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-NOV-14.
REMARK 100 THE DEPOSITION ID IS D_1000204685.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 02-JUL-13
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.0-7.0
REMARK 200 NUMBER OF CRYSTALS USED : NULL
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SOLEIL
REMARK 200 BEAMLINE : PROXIMA 1
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.97895
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : PSI PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : NULL
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13327
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.990
REMARK 200 RESOLUTION RANGE LOW (A) : 43.530
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 99.5
REMARK 200 DATA REDUNDANCY : 3.830
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 8.0800
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.99
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.10
REMARK 200 COMPLETENESS FOR SHELL (%) : 97.5
REMARK 200 DATA REDUNDANCY IN SHELL : NULL
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : NULL
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL
REMARK 200 SOFTWARE USED: SHELXDE
REMARK 200 STARTING MODEL: NULL
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM ACETATE PH 6.5, 20%
REMARK 280 PEG1500, 20% GLYCEROL, 3% METHANOL, VAPOR DIFFUSION, HANGING
REMARK 280 DROP, TEMPERATURE 293K
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 39.55000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 51.25000
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 39.55000
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 51.25000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2, 3, 4
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: 2390 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 8430 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D
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 350 APPLY THE FOLLOWING TO CHAINS: A
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 13.14507
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 164.89908
REMARK 350
REMARK 350 BIOMOLECULE: 2
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: 2280 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 8390 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -18.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 350
REMARK 350 BIOMOLECULE: 3
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: 1970 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 6830 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -16.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, F
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 350
REMARK 350 BIOMOLECULE: 4
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: 2390 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 8430 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL
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 350 APPLY THE FOLLOWING TO CHAINS: D
REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 13.14507
REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 0.00000
REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 164.89908
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 MSE A 1
REMARK 465 THR A 2
REMARK 465 SER A 3
REMARK 465 LYS A 4
REMARK 465 ARG A 5
REMARK 465 GLU A 6
REMARK 465 LYS A 7
REMARK 465 HIS A 91
REMARK 465 HIS A 92
REMARK 465 HIS A 93
REMARK 465 HIS A 94
REMARK 465 MSE B 1
REMARK 465 THR B 2
REMARK 465 SER B 3
REMARK 465 LYS B 4
REMARK 465 ARG B 5
REMARK 465 GLU B 6
REMARK 465 HIS B 91
REMARK 465 HIS B 92
REMARK 465 HIS B 93
REMARK 465 HIS B 94
REMARK 465 MSE C 1
REMARK 465 THR C 2
REMARK 465 SER C 3
REMARK 465 LYS C 4
REMARK 465 ARG C 5
REMARK 465 GLU C 6
REMARK 465 LYS C 7
REMARK 465 HIS C 89
REMARK 465 HIS C 90
REMARK 465 HIS C 91
REMARK 465 HIS C 92
REMARK 465 HIS C 93
REMARK 465 HIS C 94
REMARK 465 MSE D 1
REMARK 465 ILE D 21
REMARK 465 ARG D 22
REMARK 465 ASP D 23
REMARK 465 ASP D 24
REMARK 465 PRO D 25
REMARK 465 ARG D 26
REMARK 465 TYR D 27
REMARK 465 MSE D 28
REMARK 465 THR D 29
REMARK 465 THR D 30
REMARK 465 GLU D 31
REMARK 465 GLY D 32
REMARK 465 ARG D 33
REMARK 465 THR D 34
REMARK 465 THR D 35
REMARK 465 GLY D 36
REMARK 465 PRO D 37
REMARK 465 SER D 38
REMARK 465 ASP D 39
REMARK 465 HIS D 40
REMARK 465 VAL D 41
REMARK 465 LEU D 42
REMARK 465 ASN D 43
REMARK 465 ALA D 44
REMARK 465 GLY D 45
REMARK 465 GLN D 46
REMARK 465 ILE D 47
REMARK 465 ASP D 48
REMARK 465 ARG D 49
REMARK 465 ASP D 50
REMARK 465 LYS D 51
REMARK 465 PRO D 52
REMARK 465 SER D 53
REMARK 465 GLU D 54
REMARK 465 PRO D 55
REMARK 465 GLU D 56
REMARK 465 ARG D 57
REMARK 465 THR D 58
REMARK 465 LYS D 59
REMARK 465 ASP D 60
REMARK 465 GLY D 61
REMARK 465 SER D 62
REMARK 465 LYS D 95
REMARK 465 LYS D 96
REMARK 465 LYS D 97
REMARK 465 ALA D 98
REMARK 465 GLY D 99
REMARK 465 LEU D 113
REMARK 465 ASP D 114
REMARK 465 GLY D 115
REMARK 465 GLY D 116
REMARK 465 ASP D 117
REMARK 465 GLY D 118
REMARK 465 ASP D 119
REMARK 465 GLU D 120
REMARK 465 ASP D 121
REMARK 465 ALA D 122
REMARK 465 VAL D 123
REMARK 465 MSE E 1
REMARK 465 ILE E 21
REMARK 465 ARG E 22
REMARK 465 ASP E 23
REMARK 465 ASP E 24
REMARK 465 PRO E 25
REMARK 465 ARG E 26
REMARK 465 TYR E 27
REMARK 465 MSE E 28
REMARK 465 THR E 29
REMARK 465 THR E 30
REMARK 465 GLU E 31
REMARK 465 GLY E 32
REMARK 465 ARG E 33
REMARK 465 THR E 34
REMARK 465 THR E 35
REMARK 465 GLY E 36
REMARK 465 PRO E 37
REMARK 465 SER E 38
REMARK 465 ASP E 39
REMARK 465 HIS E 40
REMARK 465 VAL E 41
REMARK 465 LEU E 42
REMARK 465 ASN E 43
REMARK 465 ALA E 44
REMARK 465 GLY E 45
REMARK 465 GLN E 46
REMARK 465 ILE E 47
REMARK 465 ASP E 48
REMARK 465 ARG E 49
REMARK 465 ASP E 50
REMARK 465 LYS E 51
REMARK 465 PRO E 52
REMARK 465 SER E 53
REMARK 465 GLU E 54
REMARK 465 PRO E 55
REMARK 465 GLU E 56
REMARK 465 ARG E 57
REMARK 465 THR E 58
REMARK 465 LYS E 59
REMARK 465 ASP E 60
REMARK 465 GLY E 61
REMARK 465 SER E 62
REMARK 465 GLN E 63
REMARK 465 LYS E 93
REMARK 465 ASN E 94
REMARK 465 LYS E 95
REMARK 465 LYS E 96
REMARK 465 LYS E 97
REMARK 465 ALA E 98
REMARK 465 GLY E 99
REMARK 465 ALA E 100
REMARK 465 ASP E 114
REMARK 465 GLY E 115
REMARK 465 GLY E 116
REMARK 465 ASP E 117
REMARK 465 GLY E 118
REMARK 465 ASP E 119
REMARK 465 GLU E 120
REMARK 465 ASP E 121
REMARK 465 ALA E 122
REMARK 465 VAL E 123
REMARK 465 MSE F 1
REMARK 465 ILE F 21
REMARK 465 ARG F 22
REMARK 465 ASP F 23
REMARK 465 ASP F 24
REMARK 465 PRO F 25
REMARK 465 ARG F 26
REMARK 465 TYR F 27
REMARK 465 MSE F 28
REMARK 465 THR F 29
REMARK 465 THR F 30
REMARK 465 GLU F 31
REMARK 465 GLY F 32
REMARK 465 ARG F 33
REMARK 465 THR F 34
REMARK 465 THR F 35
REMARK 465 GLY F 36
REMARK 465 PRO F 37
REMARK 465 SER F 38
REMARK 465 ASP F 39
REMARK 465 HIS F 40
REMARK 465 VAL F 41
REMARK 465 LEU F 42
REMARK 465 ASN F 43
REMARK 465 ALA F 44
REMARK 465 GLY F 45
REMARK 465 GLN F 46
REMARK 465 ILE F 47
REMARK 465 ASP F 48
REMARK 465 ARG F 49
REMARK 465 ASP F 50
REMARK 465 LYS F 51
REMARK 465 PRO F 52
REMARK 465 SER F 53
REMARK 465 GLU F 54
REMARK 465 PRO F 55
REMARK 465 GLU F 56
REMARK 465 ARG F 57
REMARK 465 THR F 58
REMARK 465 LYS F 59
REMARK 465 ASP F 60
REMARK 465 GLY F 61
REMARK 465 SER F 62
REMARK 465 GLN F 63
REMARK 465 LYS F 95
REMARK 465 LYS F 96
REMARK 465 LYS F 97
REMARK 465 ALA F 98
REMARK 465 GLY F 99
REMARK 465 ALA F 100
REMARK 465 ASP F 101
REMARK 465 GLU F 102
REMARK 465 LYS F 103
REMARK 465 ARG F 104
REMARK 465 ILE F 105
REMARK 465 GLN F 106
REMARK 465 GLU F 107
REMARK 465 GLU F 108
REMARK 465 ILE F 109
REMARK 465 ASN F 110
REMARK 465 GLN F 111
REMARK 465 LEU F 112
REMARK 465 LEU F 113
REMARK 465 ASP F 114
REMARK 465 GLY F 115
REMARK 465 GLY F 116
REMARK 465 ASP F 117
REMARK 465 GLY F 118
REMARK 465 ASP F 119
REMARK 465 GLU F 120
REMARK 465 ASP F 121
REMARK 465 ALA F 122
REMARK 465 VAL F 123
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 16 CD CE NZ
REMARK 470 GLU A 22 CG CD OE1 OE2
REMARK 470 SER A 33 OG
REMARK 470 ILE A 37 CG1 CG2 CD1
REMARK 470 LEU A 38 CD1 CD2
REMARK 470 LYS A 39 CG CD CE NZ
REMARK 470 GLU A 50 CG CD OE1 OE2
REMARK 470 LYS A 51 NZ
REMARK 470 ARG A 59 NH1 NH2
REMARK 470 ILE A 61 CG1 CG2 CD1
REMARK 470 ARG A 64 CG CD NE CZ NH1 NH2
REMARK 470 VAL A 68 CG1 CG2
REMARK 470 SER A 71 OG
REMARK 470 SER A 72 OG
REMARK 470 GLU A 82 CD OE1 OE2
REMARK 470 LEU A 87 CD1 CD2
REMARK 470 LYS B 7 CG CD CE NZ
REMARK 470 SER B 8 OG
REMARK 470 THR B 21 OG1 CG2
REMARK 470 ILE B 27 CD1
REMARK 470 LYS B 30 CG CD CE NZ
REMARK 470 SER B 33 OG
REMARK 470 ILE B 37 CG1 CG2 CD1
REMARK 470 LYS B 39 CE NZ
REMARK 470 GLU B 50 OE1 OE2
REMARK 470 ARG B 64 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 67 CZ NH1 NH2
REMARK 470 ILE B 73 CD1
REMARK 470 ILE B 74 CD1
REMARK 470 ILE B 77 CD1
REMARK 470 ILE B 80 CD1
REMARK 470 GLU B 82 CD OE1 OE2
REMARK 470 LEU C 9 CD1 CD2
REMARK 470 LEU C 15 CG CD1 CD2
REMARK 470 LYS C 16 CE NZ
REMARK 470 ILE C 17 CD1
REMARK 470 GLU C 20 CG CD OE1 OE2
REMARK 470 THR C 21 OG1 CG2
REMARK 470 ARG C 23 CG CD NE CZ NH1 NH2
REMARK 470 GLN C 24 OE1 NE2
REMARK 470 ILE C 27 CG1 CG2 CD1
REMARK 470 LYS C 30 CG CD CE NZ
REMARK 470 SER C 33 OG
REMARK 470 ASP C 35 CG OD1 OD2
REMARK 470 GLN C 41 CG CD OE1 NE2
REMARK 470 SER C 48 OG
REMARK 470 LYS C 51 CE NZ
REMARK 470 LEU C 55 CG CD1 CD2
REMARK 470 ARG C 59 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 64 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 67 CG CD NE CZ NH1 NH2
REMARK 470 ILE C 73 CD1
REMARK 470 ILE C 77 CG1 CG2 CD1
REMARK 470 VAL C 81 CG1 CG2
REMARK 470 GLU C 82 CG CD OE1 OE2
REMARK 470 LYS D 2 CG CD CE NZ
REMARK 470 LEU D 3 CG CD1 CD2
REMARK 470 GLN D 63 CG CD OE1 NE2
REMARK 470 GLN D 69 CD OE1 NE2
REMARK 470 ARG D 71 CZ NH1 NH2
REMARK 470 GLU D 83 CD OE1 OE2
REMARK 470 GLU D 90 CD OE1 OE2
REMARK 470 LEU D 91 CG CD1 CD2
REMARK 470 LYS D 93 CG CD CE NZ
REMARK 470 ASN D 94 CG OD1 ND2
REMARK 470 ASP D 101 CG OD1 OD2
REMARK 470 GLU D 102 CG CD OE1 OE2
REMARK 470 LYS D 103 CG CD CE NZ
REMARK 470 ARG D 104 CG CD NE CZ NH1 NH2
REMARK 470 GLN D 106 CG CD OE1 NE2
REMARK 470 ASN D 110 CG OD1 ND2
REMARK 470 LYS E 2 CG CD CE NZ
REMARK 470 LEU E 3 CG CD1 CD2
REMARK 470 LEU E 64 CG CD1 CD2
REMARK 470 GLU E 90 CG CD OE1 OE2
REMARK 470 GLU E 102 CG CD OE1 OE2
REMARK 470 LYS E 103 CG CD CE NZ
REMARK 470 ARG E 104 CG CD NE CZ NH1 NH2
REMARK 470 GLN E 106 CG CD OE1 NE2
REMARK 470 GLU E 107 CG CD OE1 OE2
REMARK 470 GLN E 111 CG CD OE1 NE2
REMARK 470 LEU E 113 CG CD1 CD2
REMARK 470 LYS F 2 CG CD CE NZ
REMARK 470 LEU F 3 CG CD1 CD2
REMARK 470 ASP F 12 CG OD1 OD2
REMARK 470 LEU F 64 CG CD1 CD2
REMARK 470 TYR F 66 CG CD1 CD2 CE1 CE2 CZ OH
REMARK 470 LEU F 67 CG CD1 CD2
REMARK 470 GLN F 69 CG CD OE1 NE2
REMARK 470 ARG F 71 CG CD NE CZ NH1 NH2
REMARK 470 ASP F 80 OD1 OD2
REMARK 470 LYS F 93 CG CD CE NZ
REMARK 470 ASN F 94 CG OD1 ND2
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 D 7 OG SER D 17 2.10
REMARK 500 O VAL B 81 O MSE B 84 2.19
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 SER A 33 72.19 33.71
REMARK 500 PRO A 34 -77.71 -67.00
REMARK 500 ASP A 35 74.71 71.93
REMARK 500 LYS A 51 -126.53 48.41
REMARK 500 ILE A 74 -38.10 -36.49
REMARK 500 LYS B 51 -121.15 48.51
REMARK 500 MSE B 84 106.66 -57.30
REMARK 500 ASP B 85 -67.95 145.86
REMARK 500 LEU C 9 45.95 72.46
REMARK 500 LEU C 32 100.24 -57.35
REMARK 500 LYS C 51 -125.32 62.81
REMARK 500 SER C 72 -72.63 -48.57
REMARK 500 ALA D 19 122.51 -171.19
REMARK 500 TYR D 66 -73.95 -34.72
REMARK 500 GLN D 73 -30.39 -37.93
REMARK 500 ASP D 79 -70.74 -57.29
REMARK 500 ASP D 80 -62.06 -26.00
REMARK 500 LYS D 93 -71.28 -49.55
REMARK 500 ASP E 12 37.77 -88.19
REMARK 500 ALA E 19 134.44 -174.64
REMARK 500 ASP F 12 -12.04 95.00
REMARK 500 ALA F 19 117.04 -160.95
REMARK 500 TYR F 66 -70.26 -58.66
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 ACT A 101
DBREF 4WX8 A 1 88 UNP Q3E833 PCC1_YEAST 1 88
DBREF 4WX8 B 1 88 UNP Q3E833 PCC1_YEAST 1 88
DBREF 4WX8 C 1 88 UNP Q3E833 PCC1_YEAST 1 88
DBREF 4WX8 D 1 123 UNP P46984 GON7_YEAST 1 123
DBREF 4WX8 E 1 123 UNP P46984 GON7_YEAST 1 123
DBREF 4WX8 F 1 123 UNP P46984 GON7_YEAST 1 123
SEQADV 4WX8 HIS A 89 UNP Q3E833 EXPRESSION TAG
SEQADV 4WX8 HIS A 90 UNP Q3E833 EXPRESSION TAG
SEQADV 4WX8 HIS A 91 UNP Q3E833 EXPRESSION TAG
SEQADV 4WX8 HIS A 92 UNP Q3E833 EXPRESSION TAG
SEQADV 4WX8 HIS A 93 UNP Q3E833 EXPRESSION TAG
SEQADV 4WX8 HIS A 94 UNP Q3E833 EXPRESSION TAG
SEQADV 4WX8 HIS B 89 UNP Q3E833 EXPRESSION TAG
SEQADV 4WX8 HIS B 90 UNP Q3E833 EXPRESSION TAG
SEQADV 4WX8 HIS B 91 UNP Q3E833 EXPRESSION TAG
SEQADV 4WX8 HIS B 92 UNP Q3E833 EXPRESSION TAG
SEQADV 4WX8 HIS B 93 UNP Q3E833 EXPRESSION TAG
SEQADV 4WX8 HIS B 94 UNP Q3E833 EXPRESSION TAG
SEQADV 4WX8 HIS C 89 UNP Q3E833 EXPRESSION TAG
SEQADV 4WX8 HIS C 90 UNP Q3E833 EXPRESSION TAG
SEQADV 4WX8 HIS C 91 UNP Q3E833 EXPRESSION TAG
SEQADV 4WX8 HIS C 92 UNP Q3E833 EXPRESSION TAG
SEQADV 4WX8 HIS C 93 UNP Q3E833 EXPRESSION TAG
SEQADV 4WX8 HIS C 94 UNP Q3E833 EXPRESSION TAG
SEQRES 1 A 94 MSE THR SER LYS ARG GLU LYS SER LEU ASP HIS THR LEU
SEQRES 2 A 94 GLU LEU LYS ILE PRO PHE GLU THR GLU ARG GLN ALA THR
SEQRES 3 A 94 ILE ALA THR LYS VAL LEU SER PRO ASP PRO ILE LEU LYS
SEQRES 4 A 94 PRO GLN ASP PHE GLN VAL ASP TYR SER SER GLU LYS ASN
SEQRES 5 A 94 VAL MSE LEU VAL GLN PHE ARG SER ILE ASP ASP ARG VAL
SEQRES 6 A 94 LEU ARG VAL GLY VAL SER SER ILE ILE ASP SER ILE LYS
SEQRES 7 A 94 THR ILE VAL GLU ALA MSE ASP VAL LEU SER HIS HIS HIS
SEQRES 8 A 94 HIS HIS HIS
SEQRES 1 B 94 MSE THR SER LYS ARG GLU LYS SER LEU ASP HIS THR LEU
SEQRES 2 B 94 GLU LEU LYS ILE PRO PHE GLU THR GLU ARG GLN ALA THR
SEQRES 3 B 94 ILE ALA THR LYS VAL LEU SER PRO ASP PRO ILE LEU LYS
SEQRES 4 B 94 PRO GLN ASP PHE GLN VAL ASP TYR SER SER GLU LYS ASN
SEQRES 5 B 94 VAL MSE LEU VAL GLN PHE ARG SER ILE ASP ASP ARG VAL
SEQRES 6 B 94 LEU ARG VAL GLY VAL SER SER ILE ILE ASP SER ILE LYS
SEQRES 7 B 94 THR ILE VAL GLU ALA MSE ASP VAL LEU SER HIS HIS HIS
SEQRES 8 B 94 HIS HIS HIS
SEQRES 1 C 94 MSE THR SER LYS ARG GLU LYS SER LEU ASP HIS THR LEU
SEQRES 2 C 94 GLU LEU LYS ILE PRO PHE GLU THR GLU ARG GLN ALA THR
SEQRES 3 C 94 ILE ALA THR LYS VAL LEU SER PRO ASP PRO ILE LEU LYS
SEQRES 4 C 94 PRO GLN ASP PHE GLN VAL ASP TYR SER SER GLU LYS ASN
SEQRES 5 C 94 VAL MSE LEU VAL GLN PHE ARG SER ILE ASP ASP ARG VAL
SEQRES 6 C 94 LEU ARG VAL GLY VAL SER SER ILE ILE ASP SER ILE LYS
SEQRES 7 C 94 THR ILE VAL GLU ALA MSE ASP VAL LEU SER HIS HIS HIS
SEQRES 8 C 94 HIS HIS HIS
SEQRES 1 D 123 MSE LYS LEU PRO VAL ALA GLN TYR SER ALA PRO ASP GLY
SEQRES 2 D 123 VAL GLU LYS SER PHE ALA PRO ILE ARG ASP ASP PRO ARG
SEQRES 3 D 123 TYR MSE THR THR GLU GLY ARG THR THR GLY PRO SER ASP
SEQRES 4 D 123 HIS VAL LEU ASN ALA GLY GLN ILE ASP ARG ASP LYS PRO
SEQRES 5 D 123 SER GLU PRO GLU ARG THR LYS ASP GLY SER GLN LEU THR
SEQRES 6 D 123 TYR LEU GLY GLN LEU ARG THR GLN LEU THR GLY LEU GLN
SEQRES 7 D 123 ASP ASP ILE ASN GLU PHE LEU THR GLY ARG MSE GLU LEU
SEQRES 8 D 123 ALA LYS ASN LYS LYS LYS ALA GLY ALA ASP GLU LYS ARG
SEQRES 9 D 123 ILE GLN GLU GLU ILE ASN GLN LEU LEU ASP GLY GLY ASP
SEQRES 10 D 123 GLY ASP GLU ASP ALA VAL
SEQRES 1 E 123 MSE LYS LEU PRO VAL ALA GLN TYR SER ALA PRO ASP GLY
SEQRES 2 E 123 VAL GLU LYS SER PHE ALA PRO ILE ARG ASP ASP PRO ARG
SEQRES 3 E 123 TYR MSE THR THR GLU GLY ARG THR THR GLY PRO SER ASP
SEQRES 4 E 123 HIS VAL LEU ASN ALA GLY GLN ILE ASP ARG ASP LYS PRO
SEQRES 5 E 123 SER GLU PRO GLU ARG THR LYS ASP GLY SER GLN LEU THR
SEQRES 6 E 123 TYR LEU GLY GLN LEU ARG THR GLN LEU THR GLY LEU GLN
SEQRES 7 E 123 ASP ASP ILE ASN GLU PHE LEU THR GLY ARG MSE GLU LEU
SEQRES 8 E 123 ALA LYS ASN LYS LYS LYS ALA GLY ALA ASP GLU LYS ARG
SEQRES 9 E 123 ILE GLN GLU GLU ILE ASN GLN LEU LEU ASP GLY GLY ASP
SEQRES 10 E 123 GLY ASP GLU ASP ALA VAL
SEQRES 1 F 123 MSE LYS LEU PRO VAL ALA GLN TYR SER ALA PRO ASP GLY
SEQRES 2 F 123 VAL GLU LYS SER PHE ALA PRO ILE ARG ASP ASP PRO ARG
SEQRES 3 F 123 TYR MSE THR THR GLU GLY ARG THR THR GLY PRO SER ASP
SEQRES 4 F 123 HIS VAL LEU ASN ALA GLY GLN ILE ASP ARG ASP LYS PRO
SEQRES 5 F 123 SER GLU PRO GLU ARG THR LYS ASP GLY SER GLN LEU THR
SEQRES 6 F 123 TYR LEU GLY GLN LEU ARG THR GLN LEU THR GLY LEU GLN
SEQRES 7 F 123 ASP ASP ILE ASN GLU PHE LEU THR GLY ARG MSE GLU LEU
SEQRES 8 F 123 ALA LYS ASN LYS LYS LYS ALA GLY ALA ASP GLU LYS ARG
SEQRES 9 F 123 ILE GLN GLU GLU ILE ASN GLN LEU LEU ASP GLY GLY ASP
SEQRES 10 F 123 GLY ASP GLU ASP ALA VAL
MODRES 4WX8 MSE A 54 MET MODIFIED RESIDUE
MODRES 4WX8 MSE A 84 MET MODIFIED RESIDUE
MODRES 4WX8 MSE B 54 MET MODIFIED RESIDUE
MODRES 4WX8 MSE B 84 MET MODIFIED RESIDUE
MODRES 4WX8 MSE C 54 MET MODIFIED RESIDUE
MODRES 4WX8 MSE C 84 MET MODIFIED RESIDUE
MODRES 4WX8 MSE D 89 MET MODIFIED RESIDUE
MODRES 4WX8 MSE E 89 MET MODIFIED RESIDUE
MODRES 4WX8 MSE F 89 MET MODIFIED RESIDUE
HET MSE A 54 8
HET MSE A 84 8
HET MSE B 54 8
HET MSE B 84 8
HET MSE C 54 8
HET MSE C 84 8
HET MSE D 89 8
HET MSE E 89 8
HET MSE F 89 8
HET ACT A 101 4
HETNAM MSE SELENOMETHIONINE
HETNAM ACT ACETATE ION
FORMUL 1 MSE 9(C5 H11 N O2 SE)
FORMUL 7 ACT C2 H3 O2 1-
FORMUL 8 HOH *14(H2 O)
HELIX 1 AA1 THR A 21 SER A 33 1 13
HELIX 2 AA2 ASP A 62 HIS A 90 1 29
HELIX 3 AA3 THR B 21 LEU B 32 1 12
HELIX 4 AA4 ASP B 62 HIS B 90 1 29
HELIX 5 AA5 THR C 21 LEU C 32 1 12
HELIX 6 AA6 LYS C 39 GLN C 41 5 3
HELIX 7 AA7 ASP C 62 SER C 88 1 27
HELIX 8 AA8 THR D 65 ASN D 94 1 30
HELIX 9 AA9 GLU D 102 LEU D 112 1 11
HELIX 10 AB1 THR E 65 ALA E 92 1 28
HELIX 11 AB2 GLU E 102 LEU E 113 1 12
HELIX 12 AB3 THR F 65 ASN F 94 1 30
SHEET 1 AA1 3 HIS A 11 PRO A 18 0
SHEET 2 AA1 3 VAL A 53 SER A 60 -1 O VAL A 56 N LEU A 15
SHEET 3 AA1 3 PHE A 43 GLU A 50 -1 N SER A 48 O LEU A 55
SHEET 1 AA2 5 PHE B 43 GLU B 50 0
SHEET 2 AA2 5 VAL B 53 SER B 60 -1 O LEU B 55 N SER B 48
SHEET 3 AA2 5 HIS B 11 PRO B 18 -1 N HIS B 11 O SER B 60
SHEET 4 AA2 5 VAL E 5 SER E 9 -1 O GLN E 7 N GLU B 14
SHEET 5 AA2 5 GLU E 15 PHE E 18 -1 O PHE E 18 N ALA E 6
SHEET 1 AA3 7 PHE C 43 GLU C 50 0
SHEET 2 AA3 7 VAL C 53 SER C 60 -1 O LEU C 55 N SER C 48
SHEET 3 AA3 7 HIS C 11 PRO C 18 -1 N LEU C 13 O PHE C 58
SHEET 4 AA3 7 VAL F 5 SER F 9 -1 O SER F 9 N THR C 12
SHEET 5 AA3 7 VAL F 14 PHE F 18 -1 O PHE F 18 N ALA F 6
SHEET 6 AA3 7 VAL D 14 PHE D 18 -1 N GLU D 15 O GLU F 15
SHEET 7 AA3 7 ALA D 6 ALA D 10 -1 N TYR D 8 O LYS D 16
LINK C VAL A 53 N MSE A 54 1555 1555 1.33
LINK C MSE A 54 N LEU A 55 1555 1555 1.32
LINK C ALA A 83 N MSE A 84 1555 1555 1.33
LINK C MSE A 84 N ASP A 85 1555 1555 1.34
LINK C VAL B 53 N MSE B 54 1555 1555 1.33
LINK C MSE B 54 N LEU B 55 1555 1555 1.33
LINK C ALA B 83 N MSE B 84 1555 1555 1.33
LINK C MSE B 84 N ASP B 85 1555 1555 1.31
LINK C VAL C 53 N MSE C 54 1555 1555 1.34
LINK C MSE C 54 N LEU C 55 1555 1555 1.32
LINK C ALA C 83 N MSE C 84 1555 1555 1.33
LINK C MSE C 84 N ASP C 85 1555 1555 1.33
LINK C ARG D 88 N MSE D 89 1555 1555 1.33
LINK C MSE D 89 N GLU D 90 1555 1555 1.33
LINK C ARG E 88 N MSE E 89 1555 1555 1.33
LINK C MSE E 89 N GLU E 90 1555 1555 1.33
LINK C ARG F 88 N MSE F 89 1555 1555 1.33
LINK C MSE F 89 N GLU F 90 1555 1555 1.32
SITE 1 AC1 4 ASP A 46 SER A 48 LEU A 55 GLN A 57
CRYST1 79.100 102.500 88.800 90.00 111.80 90.00 C 1 2 1 12
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 0.012642 0.000000 0.005057 0.00000
SCALE2 0.000000 0.009756 0.000000 0.00000
SCALE3 0.000000 0.000000 0.012129 0.00000
MTRIX1 1 1.000000 0.000000 0.000000 0.00000 1
MTRIX2 1 0.000000 1.000000 0.000000 0.00000 1
MTRIX3 1 0.000000 0.000000 1.000000 0.00000 1
MTRIX1 2 -0.162983 0.881485 0.443194 -73.66135 1
MTRIX2 2 -0.882217 -0.331321 0.334544 53.51404 1
MTRIX3 2 0.441735 -0.336468 0.831661 45.65115 1
MTRIX1 3 -0.548240 -0.590229 0.592505 6.01756 1
MTRIX2 3 0.584933 -0.776969 -0.232751 115.58437 1
MTRIX3 3 0.597734 0.218972 0.771210 33.65894 1
MTRIX1 4 1.000000 0.000000 0.000000 0.00000 1
MTRIX2 4 0.000000 1.000000 0.000000 0.00000 1
MTRIX3 4 0.000000 0.000000 1.000000 0.00000 1
MTRIX1 5 0.150449 -0.878948 -0.452565 87.29021 1
MTRIX2 5 -0.880888 -0.326988 0.342220 52.82147 1
MTRIX3 5 -0.448777 0.347173 -0.823450 118.23556 1
(ATOM LINES ARE NOT SHOWN.)
END
