HEADER HYDROLASE 11-JUN-12 4FJC
TITLE STRUCTURE OF THE SAGA UBP8/SGF11(1-72, DELTA-ZNF)/SUS1/SGF73 DUB
TITLE 2 MODULE
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 8;
COMPND 3 CHAIN: A, E;
COMPND 4 SYNONYM: DEUBIQUITINATING ENZYME 8, UBIQUITIN THIOESTERASE 8,
COMPND 5 UBIQUITIN-SPECIFIC-PROCESSING PROTEASE 8;
COMPND 6 EC: 3.4.19.12;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: PROTEIN SUS1;
COMPND 10 CHAIN: B, F;
COMPND 11 ENGINEERED: YES;
COMPND 12 MOL_ID: 3;
COMPND 13 MOLECULE: SAGA-ASSOCIATED FACTOR 11;
COMPND 14 CHAIN: C, G;
COMPND 15 FRAGMENT: UNP RESIDUES SGF11 1-72;
COMPND 16 SYNONYM: 11 KDA SAGA-ASSOCIATED FACTOR;
COMPND 17 ENGINEERED: YES;
COMPND 18 MOL_ID: 4;
COMPND 19 MOLECULE: SAGA-ASSOCIATED FACTOR 73;
COMPND 20 CHAIN: D, H;
COMPND 21 FRAGMENT: UNP RESIDUES 1-96;
COMPND 22 SYNONYM: 73 KDA SAGA-ASSOCIATED FACTOR, SAGA HISTONE
COMPND 23 ACETYLTRANSFERASE COMPLEX 73 KDA SUBUNIT;
COMPND 24 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: UBP8, YM9959.05, YMR223W;
SOURCE 7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 9 EXPRESSION_SYSTEM_STRAIN: ROSETTA2(DE3) PLYSS;
SOURCE 10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 11 EXPRESSION_SYSTEM_PLASMID: PET-32A;
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: SUS1, YBR111W-A;
SOURCE 18 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 19 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 20 EXPRESSION_SYSTEM_STRAIN: ROSETTA2(DE3) PLYSS;
SOURCE 21 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 22 EXPRESSION_SYSTEM_PLASMID: PRSF;
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: SGF11, YPL047W;
SOURCE 29 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 30 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 31 EXPRESSION_SYSTEM_STRAIN: ROSETTA2(DE3) PLYSS;
SOURCE 32 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 33 EXPRESSION_SYSTEM_PLASMID: PCDFDUET-1;
SOURCE 34 MOL_ID: 4;
SOURCE 35 ORGANISM_SCIENTIFIC: SACCHAROMYCES CEREVISIAE;
SOURCE 36 ORGANISM_COMMON: BAKER'S YEAST;
SOURCE 37 ORGANISM_TAXID: 559292;
SOURCE 38 STRAIN: ATCC 204508 / S288C;
SOURCE 39 GENE: SGF73, YGL066W;
SOURCE 40 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 41 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 42 EXPRESSION_SYSTEM_STRAIN: ROSETTA2(DE3) PLYSS;
SOURCE 43 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 44 EXPRESSION_SYSTEM_PLASMID: PCDFDUET-1
KEYWDS DOMAIN-SWAPPING, DEUBIQUITINATION, TRANSCRIPTION, NUCLEOSOME,
KEYWDS 2 HYDROLASE
EXPDTA X-RAY DIFFRACTION
AUTHOR N.L.SAMARA,A.E.RINGEL,C.WOLBERGER
REVDAT 3 13-SEP-23 4FJC 1 REMARK SEQADV LINK
REVDAT 2 29-AUG-12 4FJC 1 JRNL
REVDAT 1 25-JUL-12 4FJC 0
JRNL AUTH N.L.SAMARA,A.E.RINGEL,C.WOLBERGER
JRNL TITL A ROLE FOR INTERSUBUNIT INTERACTIONS IN MAINTAINING SAGA
JRNL TITL 2 DEUBIQUITINATING MODULE STRUCTURE AND ACTIVITY.
JRNL REF STRUCTURE V. 20 1414 2012
JRNL REFN ISSN 0969-2126
JRNL PMID 22771212
JRNL DOI 10.1016/J.STR.2012.05.015
REMARK 2
REMARK 2 RESOLUTION. 2.83 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.6.0117
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.83
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 265.94
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 96.3
REMARK 3 NUMBER OF REFLECTIONS : 36236
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) : 0.204
REMARK 3 R VALUE (WORKING SET) : 0.200
REMARK 3 FREE R VALUE : 0.276
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 1909
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) : 2.83
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.90
REMARK 3 REFLECTION IN BIN (WORKING SET) : 2065
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 80.92
REMARK 3 BIN R VALUE (WORKING SET) : 0.3330
REMARK 3 BIN FREE R VALUE SET COUNT : 111
REMARK 3 BIN FREE R VALUE : 0.4210
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 10515
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 20
REMARK 3 SOLVENT ATOMS : 46
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 41.51
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 1.56000
REMARK 3 B22 (A**2) : 1.12000
REMARK 3 B33 (A**2) : -2.68000
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 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.434
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.316
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 34.879
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.934
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.880
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 10714 ; 0.011 ; 0.020
REMARK 3 BOND LENGTHS OTHERS (A): 7246 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 14444 ; 1.436 ; 1.953
REMARK 3 BOND ANGLES OTHERS (DEGREES): 17815 ; 0.909 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1292 ; 7.152 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 508 ;39.628 ;25.551
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1997 ;18.313 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 33 ;13.584 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1622 ; 0.078 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 11680 ; 0.005 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 2021 ; 0.001 ; 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): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
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 : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 8
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 0 A 471
REMARK 3 RESIDUE RANGE : A 501 A 507
REMARK 3 RESIDUE RANGE : A 601 A 616
REMARK 3 ORIGIN FOR THE GROUP (A): -21.4797 -11.7402 31.2110
REMARK 3 T TENSOR
REMARK 3 T11: 0.2376 T22: 0.1905
REMARK 3 T33: 0.2089 T12: 0.0815
REMARK 3 T13: -0.0047 T23: 0.0200
REMARK 3 L TENSOR
REMARK 3 L11: 0.0916 L22: 0.5690
REMARK 3 L33: 1.1857 L12: 0.1563
REMARK 3 L13: 0.1087 L23: 0.7274
REMARK 3 S TENSOR
REMARK 3 S11: -0.0041 S12: 0.0041 S13: 0.0198
REMARK 3 S21: 0.0272 S22: -0.0003 S23: 0.0925
REMARK 3 S31: 0.0179 S32: -0.0270 S33: 0.0044
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 5 B 96
REMARK 3 ORIGIN FOR THE GROUP (A): -5.1683 -45.0218 -10.9582
REMARK 3 T TENSOR
REMARK 3 T11: 0.1377 T22: 0.2005
REMARK 3 T33: 0.2568 T12: -0.0035
REMARK 3 T13: -0.0105 T23: -0.0079
REMARK 3 L TENSOR
REMARK 3 L11: 0.5907 L22: 2.6393
REMARK 3 L33: 1.2747 L12: -0.7954
REMARK 3 L13: -0.5062 L23: 0.4995
REMARK 3 S TENSOR
REMARK 3 S11: -0.1659 S12: 0.0190 S13: 0.0899
REMARK 3 S21: 0.0487 S22: 0.1530 S23: -0.1388
REMARK 3 S31: 0.1183 S32: 0.2846 S33: 0.0129
REMARK 3
REMARK 3 TLS GROUP : 3
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 3 C 45
REMARK 3 RESIDUE RANGE : C 101 C 101
REMARK 3 ORIGIN FOR THE GROUP (A): -11.1295 -36.4804 -11.0334
REMARK 3 T TENSOR
REMARK 3 T11: 0.3283 T22: 0.2573
REMARK 3 T33: 0.2613 T12: -0.1253
REMARK 3 T13: -0.0341 T23: -0.0848
REMARK 3 L TENSOR
REMARK 3 L11: 2.3628 L22: 2.2569
REMARK 3 L33: 0.6057 L12: -1.8626
REMARK 3 L13: -1.1036 L23: 1.0306
REMARK 3 S TENSOR
REMARK 3 S11: -0.2078 S12: -0.2283 S13: 0.1854
REMARK 3 S21: -0.3012 S22: 0.3735 S23: 0.0555
REMARK 3 S31: -0.0394 S32: 0.2423 S33: -0.1657
REMARK 3
REMARK 3 TLS GROUP : 4
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 5 D 96
REMARK 3 RESIDUE RANGE : D 101 D 101
REMARK 3 RESIDUE RANGE : D 201 D 205
REMARK 3 ORIGIN FOR THE GROUP (A): -22.8959 -47.3442 -1.6656
REMARK 3 T TENSOR
REMARK 3 T11: 0.2474 T22: 0.1962
REMARK 3 T33: 0.2429 T12: -0.0370
REMARK 3 T13: -0.0252 T23: -0.0114
REMARK 3 L TENSOR
REMARK 3 L11: 0.1737 L22: 0.8603
REMARK 3 L33: 0.8623 L12: -0.1527
REMARK 3 L13: -0.3363 L23: 0.5050
REMARK 3 S TENSOR
REMARK 3 S11: -0.1614 S12: -0.0148 S13: 0.0276
REMARK 3 S21: -0.0511 S22: 0.2001 S23: 0.2065
REMARK 3 S31: 0.1601 S32: 0.0181 S33: -0.0387
REMARK 3
REMARK 3 TLS GROUP : 5
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : E 0 E 471
REMARK 3 RESIDUE RANGE : E 501 E 506
REMARK 3 RESIDUE RANGE : E 601 E 620
REMARK 3 ORIGIN FOR THE GROUP (A): -14.3459 -32.3071 43.0517
REMARK 3 T TENSOR
REMARK 3 T11: 0.2799 T22: 0.3315
REMARK 3 T33: 0.1866 T12: 0.1422
REMARK 3 T13: -0.0142 T23: -0.0121
REMARK 3 L TENSOR
REMARK 3 L11: 0.0221 L22: 0.0691
REMARK 3 L33: 0.0367 L12: 0.0190
REMARK 3 L13: -0.0064 L23: 0.0260
REMARK 3 S TENSOR
REMARK 3 S11: -0.0074 S12: -0.0259 S13: -0.0405
REMARK 3 S21: 0.0541 S22: -0.0440 S23: 0.0270
REMARK 3 S31: 0.0392 S32: 0.0531 S33: 0.0515
REMARK 3
REMARK 3 TLS GROUP : 6
REMARK 3 NUMBER OF COMPONENTS GROUP : 2
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : F 7 F 93
REMARK 3 RESIDUE RANGE : F 101 F 102
REMARK 3 ORIGIN FOR THE GROUP (A): -10.0217 6.5815 82.6063
REMARK 3 T TENSOR
REMARK 3 T11: 0.1304 T22: 0.3186
REMARK 3 T33: 0.1164 T12: -0.1002
REMARK 3 T13: 0.0220 T23: 0.0616
REMARK 3 L TENSOR
REMARK 3 L11: 0.3089 L22: 3.8289
REMARK 3 L33: 3.3184 L12: -0.7549
REMARK 3 L13: -0.5595 L23: -0.7656
REMARK 3 S TENSOR
REMARK 3 S11: 0.1168 S12: -0.1106 S13: -0.0395
REMARK 3 S21: 0.0863 S22: -0.2154 S23: 0.0516
REMARK 3 S31: -0.5995 S32: 0.7456 S33: 0.0986
REMARK 3
REMARK 3 TLS GROUP : 7
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : G 5 G 45
REMARK 3 ORIGIN FOR THE GROUP (A): -10.8021 -3.9347 82.9206
REMARK 3 T TENSOR
REMARK 3 T11: 0.2885 T22: 0.6134
REMARK 3 T33: 0.0269 T12: 0.1870
REMARK 3 T13: -0.0180 T23: -0.0262
REMARK 3 L TENSOR
REMARK 3 L11: 0.1361 L22: 6.4193
REMARK 3 L33: 2.4291 L12: 0.0735
REMARK 3 L13: -0.4055 L23: 2.5394
REMARK 3 S TENSOR
REMARK 3 S11: -0.1554 S12: -0.2779 S13: 0.0185
REMARK 3 S21: 0.0127 S22: 0.2305 S23: 0.0465
REMARK 3 S31: 0.3032 S32: 1.0316 S33: -0.0751
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 3
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : H 9 H 95
REMARK 3 RESIDUE RANGE : H 101 H 101
REMARK 3 RESIDUE RANGE : H 201 H 202
REMARK 3 ORIGIN FOR THE GROUP (A): -28.1122 -2.5199 75.1438
REMARK 3 T TENSOR
REMARK 3 T11: 0.2354 T22: 0.4007
REMARK 3 T33: 0.1111 T12: 0.0074
REMARK 3 T13: 0.0719 T23: -0.0189
REMARK 3 L TENSOR
REMARK 3 L11: 0.2829 L22: 0.2692
REMARK 3 L33: 1.1605 L12: -0.0271
REMARK 3 L13: -0.3425 L23: 0.4215
REMARK 3 S TENSOR
REMARK 3 S11: -0.0207 S12: 0.0546 S13: 0.0307
REMARK 3 S21: 0.0211 S22: 0.0091 S23: -0.0260
REMARK 3 S31: 0.1157 S32: -0.3365 S33: 0.0117
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 4FJC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-JUN-12.
REMARK 100 THE DEPOSITION ID IS D_1000072970.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 22-JUL-11
REMARK 200 TEMPERATURE (KELVIN) : 108
REMARK 200 PH : 8
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : APS
REMARK 200 BEAMLINE : 23-ID-B
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0332
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL CRYO-COOLED
REMARK 200 SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : MARMOSAIC 300 MM CCD
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-2000
REMARK 200 DATA SCALING SOFTWARE : HKL-2000
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 38300
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.826
REMARK 200 RESOLUTION RANGE LOW (A) : 265.943
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 96.8
REMARK 200 DATA REDUNDANCY : NULL
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : NULL
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.83
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.90
REMARK 200 COMPLETENESS FOR SHELL (%) : 94.7
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: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: MOLREP
REMARK 200 STARTING MODEL: PDB ENTRY 4FIP
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 46.71
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.31
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 14% PEG3350, 0.18-0.22 M TRI-AMMONIUM
REMARK 280 CITRATE, 8-14% GLYCEROL, VAPOR DIFFUSION, HANGING DROP,
REMARK 280 TEMPERATURE 291K, PH 8
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 38.24500
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 132.97150
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 39.60100
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 132.97150
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 38.24500
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 39.60100
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 300 REMARK: THE BIOLOGICAL ASSEMBLY IS AN OCTAMER DERIVED FROM A DOMAIN-
REMARK 300 SWAPPED DIMER OF A TETRAMERIC COMPLEX.
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: OCTAMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 33310 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 59040 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -264.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H
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 -4
REMARK 465 ALA A -3
REMARK 465 ALA A -2
REMARK 465 ALA A -1
REMARK 465 LEU A 198
REMARK 465 ASN A 199
REMARK 465 THR A 200
REMARK 465 LYS A 201
REMARK 465 GLN A 202
REMARK 465 ALA A 203
REMARK 465 SER A 204
REMARK 465 SER A 205
REMARK 465 SER A 206
REMARK 465 SER A 207
REMARK 465 THR A 208
REMARK 465 SER A 209
REMARK 465 GLU A 262
REMARK 465 VAL A 263
REMARK 465 GLY A 337
REMARK 465 LYS A 395
REMARK 465 GLU A 396
REMARK 465 LYS A 397
REMARK 465 ASP A 398
REMARK 465 LYS A 399
REMARK 465 HIS A 400
REMARK 465 SER A 401
REMARK 465 GLU A 402
REMARK 465 ASN A 403
REMARK 465 GLY A 404
REMARK 465 MET B 1
REMARK 465 THR B 2
REMARK 465 MET B 3
REMARK 465 ASP B 4
REMARK 465 MET C 1
REMARK 465 THR C 2
REMARK 465 ARG C 46
REMARK 465 SER C 47
REMARK 465 TYR C 48
REMARK 465 TYR C 49
REMARK 465 PHE C 50
REMARK 465 ASP C 51
REMARK 465 PRO C 52
REMARK 465 ASN C 53
REMARK 465 GLY C 54
REMARK 465 SER C 55
REMARK 465 LEU C 56
REMARK 465 ASP C 57
REMARK 465 ILE C 58
REMARK 465 ASN C 59
REMARK 465 GLY C 60
REMARK 465 LEU C 61
REMARK 465 GLN C 62
REMARK 465 LYS C 63
REMARK 465 GLN C 64
REMARK 465 GLN C 65
REMARK 465 GLU C 66
REMARK 465 SER C 67
REMARK 465 SER C 68
REMARK 465 GLN C 69
REMARK 465 TYR C 70
REMARK 465 ILE C 71
REMARK 465 HIS C 72
REMARK 465 CYS C 73
REMARK 465 GLU C 74
REMARK 465 ASN C 75
REMARK 465 CYS C 76
REMARK 465 GLY C 77
REMARK 465 ARG C 78
REMARK 465 ASP C 79
REMARK 465 VAL C 80
REMARK 465 SER C 81
REMARK 465 ALA C 82
REMARK 465 ASN C 83
REMARK 465 ARG C 84
REMARK 465 LEU C 85
REMARK 465 ALA C 86
REMARK 465 ALA C 87
REMARK 465 HIS C 88
REMARK 465 LEU C 89
REMARK 465 GLN C 90
REMARK 465 ARG C 91
REMARK 465 CYS C 92
REMARK 465 LEU C 93
REMARK 465 SER C 94
REMARK 465 ARG C 95
REMARK 465 GLY C 96
REMARK 465 ALA C 97
REMARK 465 ARG C 98
REMARK 465 ARG C 99
REMARK 465 MET D 1
REMARK 465 ARG D 2
REMARK 465 SER D 3
REMARK 465 GLY D 4
REMARK 465 GLY D 24
REMARK 465 SER D 25
REMARK 465 GLY E -4
REMARK 465 ALA E -3
REMARK 465 ALA E -2
REMARK 465 ALA E -1
REMARK 465 ILE E 140
REMARK 465 ASN E 141
REMARK 465 MET E 142
REMARK 465 GLY E 143
REMARK 465 THR E 200
REMARK 465 LYS E 201
REMARK 465 GLN E 202
REMARK 465 ALA E 203
REMARK 465 SER E 204
REMARK 465 SER E 205
REMARK 465 SER E 206
REMARK 465 SER E 207
REMARK 465 THR E 208
REMARK 465 SER E 209
REMARK 465 THR E 210
REMARK 465 ALA E 260
REMARK 465 LYS E 261
REMARK 465 GLU E 262
REMARK 465 VAL E 263
REMARK 465 SER E 264
REMARK 465 ARG E 265
REMARK 465 ALA E 266
REMARK 465 ASN E 267
REMARK 465 ASN E 268
REMARK 465 LEU E 369
REMARK 465 ASN E 370
REMARK 465 GLY E 371
REMARK 465 SER E 372
REMARK 465 LYS E 395
REMARK 465 GLU E 396
REMARK 465 LYS E 397
REMARK 465 ASP E 398
REMARK 465 LYS E 399
REMARK 465 HIS E 400
REMARK 465 SER E 401
REMARK 465 GLU E 402
REMARK 465 ASN E 403
REMARK 465 GLY E 404
REMARK 465 MET F 1
REMARK 465 THR F 2
REMARK 465 MET F 3
REMARK 465 ASP F 4
REMARK 465 THR F 5
REMARK 465 ALA F 6
REMARK 465 ASP F 94
REMARK 465 THR F 95
REMARK 465 GLN F 96
REMARK 465 MET G 1
REMARK 465 THR G 2
REMARK 465 GLU G 3
REMARK 465 GLU G 4
REMARK 465 ARG G 46
REMARK 465 SER G 47
REMARK 465 TYR G 48
REMARK 465 TYR G 49
REMARK 465 PHE G 50
REMARK 465 ASP G 51
REMARK 465 PRO G 52
REMARK 465 ASN G 53
REMARK 465 GLY G 54
REMARK 465 SER G 55
REMARK 465 LEU G 56
REMARK 465 ASP G 57
REMARK 465 ILE G 58
REMARK 465 ASN G 59
REMARK 465 GLY G 60
REMARK 465 LEU G 61
REMARK 465 GLN G 62
REMARK 465 LYS G 63
REMARK 465 GLN G 64
REMARK 465 GLN G 65
REMARK 465 GLU G 66
REMARK 465 SER G 67
REMARK 465 SER G 68
REMARK 465 GLN G 69
REMARK 465 TYR G 70
REMARK 465 ILE G 71
REMARK 465 HIS G 72
REMARK 465 CYS G 73
REMARK 465 GLU G 74
REMARK 465 ASN G 75
REMARK 465 CYS G 76
REMARK 465 GLY G 77
REMARK 465 ARG G 78
REMARK 465 ASP G 79
REMARK 465 VAL G 80
REMARK 465 SER G 81
REMARK 465 ALA G 82
REMARK 465 ASN G 83
REMARK 465 ARG G 84
REMARK 465 LEU G 85
REMARK 465 ALA G 86
REMARK 465 ALA G 87
REMARK 465 HIS G 88
REMARK 465 LEU G 89
REMARK 465 GLN G 90
REMARK 465 ARG G 91
REMARK 465 CYS G 92
REMARK 465 LEU G 93
REMARK 465 SER G 94
REMARK 465 ARG G 95
REMARK 465 GLY G 96
REMARK 465 ALA G 97
REMARK 465 ARG G 98
REMARK 465 ARG G 99
REMARK 465 MET H 1
REMARK 465 ARG H 2
REMARK 465 SER H 3
REMARK 465 GLY H 4
REMARK 465 ASP H 5
REMARK 465 ALA H 6
REMARK 465 GLU H 7
REMARK 465 ILE H 8
REMARK 465 SER H 20
REMARK 465 LEU H 21
REMARK 465 SER H 22
REMARK 465 GLN H 23
REMARK 465 GLY H 24
REMARK 465 SER H 25
REMARK 465 GLY H 26
REMARK 465 PRO H 27
REMARK 465 SER H 28
REMARK 465 ASN H 29
REMARK 465 ASN H 96
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 GLU A 381 OE2
REMARK 470 GLU H 95 O
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 HIS A 50 14.34 54.79
REMARK 500 ASN A 91 5.70 -154.72
REMARK 500 SER A 137 144.85 179.83
REMARK 500 ILE A 140 103.67 -58.90
REMARK 500 GLN A 168 14.00 57.25
REMARK 500 TYR A 233 32.20 -74.56
REMARK 500 LYS A 326 103.85 -58.74
REMARK 500 CYS A 339 -79.49 -133.64
REMARK 500 THR A 342 -73.87 -75.53
REMARK 500 LEU A 368 -167.20 -111.84
REMARK 500 ASN A 370 -148.56 53.06
REMARK 500 ASP A 408 123.39 -39.91
REMARK 500 ASP A 444 113.13 -32.57
REMARK 500 ARG A 468 -50.22 -128.42
REMARK 500 GLN B 7 55.77 -117.17
REMARK 500 GLU B 54 56.95 36.62
REMARK 500 LEU D 44 140.80 -37.72
REMARK 500 GLU D 95 43.20 -83.40
REMARK 500 SER E 54 71.25 -69.82
REMARK 500 ALA E 56 157.25 -47.89
REMARK 500 GLN E 62 -27.99 -152.85
REMARK 500 ASN E 90 -70.09 -81.28
REMARK 500 LEU E 114 42.68 -108.75
REMARK 500 TYR E 117 14.40 -141.30
REMARK 500 SER E 137 129.86 -173.87
REMARK 500 ARG E 177 67.24 37.87
REMARK 500 SER E 178 130.59 179.41
REMARK 500 LEU E 230 133.32 168.60
REMARK 500 GLN E 236 64.78 -62.89
REMARK 500 PRO E 258 39.13 -91.13
REMARK 500 PRO E 302 155.98 -48.76
REMARK 500 ASN E 424 -65.57 71.03
REMARK 500 GLU E 425 24.08 -78.70
REMARK 500 ASN E 443 79.22 -113.66
REMARK 500 SER E 445 -9.19 83.70
REMARK 500 ARG E 468 -48.68 -130.77
REMARK 500 GLU F 54 16.96 45.24
REMARK 500 GLU F 91 -63.11 -24.39
REMARK 500 PRO G 43 3.62 -68.08
REMARK 500 LEU H 44 125.22 -30.01
REMARK 500 HIS H 48 35.82 -149.97
REMARK 500 LEU H 87 -45.12 -29.05
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS
REMARK 500
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH
REMARK 500 CIS AND TRANS CONFORMATION. CIS BONDS, IF ANY, ARE LISTED
REMARK 500 ON CISPEP RECORDS. TRANS IS DEFINED AS 180 +/- 30 AND
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.
REMARK 500 MODEL OMEGA
REMARK 500 GLY A 232 TYR A 233 -148.05
REMARK 500 SER D 28 ASN D 29 145.78
REMARK 500 ASN E 227 GLN E 228 -30.85
REMARK 500 GLU E 366 HIS E 367 -147.91
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 4 SG
REMARK 620 2 HIS A 6 ND1 109.3
REMARK 620 3 CYS A 96 SG 115.7 114.8
REMARK 620 4 CYS A 99 SG 106.1 98.7 110.6
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 502 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 46 SG
REMARK 620 2 CYS A 49 SG 106.2
REMARK 620 3 CYS A 68 SG 114.3 124.7
REMARK 620 4 HIS A 73 ND1 99.6 106.5 102.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 503 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 60 SG
REMARK 620 2 CYS A 63 SG 109.1
REMARK 620 3 HIS A 77 NE2 120.4 107.5
REMARK 620 4 HIS A 83 ND1 96.1 117.6 106.4
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 504 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 HIS A 170 NE2
REMARK 620 2 CYS A 174 SG 78.0
REMARK 620 3 CYS A 182 SG 90.5 84.3
REMARK 620 4 CYS A 185 SG 116.9 134.7 134.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 505 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 271 SG
REMARK 620 2 CYS A 273 SG 113.6
REMARK 620 3 HIS A 276 ND1 95.5 121.8
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN A 506 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 289 SG
REMARK 620 2 CYS A 336 SG 81.9
REMARK 620 N 1
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN D 101 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS D 78 SG
REMARK 620 2 CYS D 81 SG 100.0
REMARK 620 3 HIS D 93 NE2 104.3 92.5
REMARK 620 4 HOH D 203 O 115.3 128.3 112.3
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN E 501 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS E 4 SG
REMARK 620 2 HIS E 6 ND1 111.8
REMARK 620 3 CYS E 96 SG 125.1 99.2
REMARK 620 4 CYS E 99 SG 118.4 90.2 105.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN E 502 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS E 46 SG
REMARK 620 2 CYS E 68 SG 102.6
REMARK 620 3 HIS E 73 ND1 107.9 101.4
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN E 503 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS E 60 SG
REMARK 620 2 CYS E 63 SG 118.1
REMARK 620 3 HIS E 77 NE2 108.7 100.0
REMARK 620 4 HIS E 83 ND1 94.3 129.3 105.2
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN E 504 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS E 174 SG
REMARK 620 2 CYS E 182 SG 120.6
REMARK 620 3 CYS E 185 SG 106.0 101.6
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN E 505 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS E 271 SG
REMARK 620 2 CYS E 273 SG 106.2
REMARK 620 3 HIS E 276 ND1 118.2 94.8
REMARK 620 N 1 2
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN E 506 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS E 289 SG
REMARK 620 2 CYS E 292 SG 123.5
REMARK 620 3 CYS E 336 SG 105.3 104.7
REMARK 620 4 CYS E 339 SG 106.9 117.5 94.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN H 101 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS H 78 SG
REMARK 620 2 CYS H 81 SG 98.4
REMARK 620 N 1
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
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 507
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN D 101
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 501
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 502
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 503
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 504
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 505
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 506
REMARK 800
REMARK 800 SITE_IDENTIFIER: BC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN H 101
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 4FIP RELATED DB: PDB
REMARK 900 SAME COMPLEX BUT WITH AN S144N MUTATION IN UBP8.
DBREF 4FJC A 1 471 UNP P50102 UBP8_YEAST 1 471
DBREF 4FJC B 1 96 UNP Q6WNK7 SUS1_YEAST 1 96
DBREF 4FJC C 1 99 UNP Q03067 SGF11_YEAST 1 99
DBREF 4FJC D 1 96 UNP P53165 SGF73_YEAST 1 96
DBREF 4FJC E 1 471 UNP P50102 UBP8_YEAST 1 471
DBREF 4FJC F 1 96 UNP Q6WNK7 SUS1_YEAST 1 96
DBREF 4FJC G 1 99 UNP Q03067 SGF11_YEAST 1 99
DBREF 4FJC H 1 96 UNP P53165 SGF73_YEAST 1 96
SEQADV 4FJC GLY A -4 UNP P50102 EXPRESSION TAG
SEQADV 4FJC ALA A -3 UNP P50102 EXPRESSION TAG
SEQADV 4FJC ALA A -2 UNP P50102 EXPRESSION TAG
SEQADV 4FJC ALA A -1 UNP P50102 EXPRESSION TAG
SEQADV 4FJC ALA A 0 UNP P50102 EXPRESSION TAG
SEQADV 4FJC GLY E -4 UNP P50102 EXPRESSION TAG
SEQADV 4FJC ALA E -3 UNP P50102 EXPRESSION TAG
SEQADV 4FJC ALA E -2 UNP P50102 EXPRESSION TAG
SEQADV 4FJC ALA E -1 UNP P50102 EXPRESSION TAG
SEQADV 4FJC ALA E 0 UNP P50102 EXPRESSION TAG
SEQRES 1 A 476 GLY ALA ALA ALA ALA MET SER ILE CYS PRO HIS ILE GLN
SEQRES 2 A 476 GLN VAL PHE GLN ASN GLU LYS SER LYS ASP GLY VAL LEU
SEQRES 3 A 476 LYS THR CYS ASN ALA ALA ARG TYR ILE LEU ASN HIS SER
SEQRES 4 A 476 VAL PRO LYS GLU LYS PHE LEU ASN THR MET LYS CYS GLY
SEQRES 5 A 476 THR CYS HIS GLU ILE ASN SER GLY ALA THR PHE MET CYS
SEQRES 6 A 476 LEU GLN CYS GLY PHE CYS GLY CYS TRP ASN HIS SER HIS
SEQRES 7 A 476 PHE LEU SER HIS SER LYS GLN ILE GLY HIS ILE PHE GLY
SEQRES 8 A 476 ILE ASN SER ASN ASN GLY LEU LEU PHE CYS PHE LYS CYS
SEQRES 9 A 476 GLU ASP TYR ILE GLY ASN ILE ASP LEU ILE ASN ASP ALA
SEQRES 10 A 476 ILE LEU ALA LYS TYR TRP ASP ASP VAL CYS THR LYS THR
SEQRES 11 A 476 MET VAL PRO SER MET GLU ARG ARG ASP GLY LEU SER GLY
SEQRES 12 A 476 LEU ILE ASN MET GLY SER THR CYS PHE MET SER SER ILE
SEQRES 13 A 476 LEU GLN CYS LEU ILE HIS ASN PRO TYR PHE ILE ARG HIS
SEQRES 14 A 476 SER MET SER GLN ILE HIS SER ASN ASN CYS LYS VAL ARG
SEQRES 15 A 476 SER PRO ASP LYS CYS PHE SER CYS ALA LEU ASP LYS ILE
SEQRES 16 A 476 VAL HIS GLU LEU TYR GLY ALA LEU ASN THR LYS GLN ALA
SEQRES 17 A 476 SER SER SER SER THR SER THR ASN ARG GLN THR GLY PHE
SEQRES 18 A 476 ILE TYR LEU LEU THR CYS ALA TRP LYS ILE ASN GLN ASN
SEQRES 19 A 476 LEU ALA GLY TYR SER GLN GLN ASP ALA HIS GLU PHE TRP
SEQRES 20 A 476 GLN PHE ILE ILE ASN GLN ILE HIS GLN SER TYR VAL LEU
SEQRES 21 A 476 ASP LEU PRO ASN ALA LYS GLU VAL SER ARG ALA ASN ASN
SEQRES 22 A 476 LYS GLN CYS GLU CYS ILE VAL HIS THR VAL PHE GLU GLY
SEQRES 23 A 476 SER LEU GLU SER SER ILE VAL CYS PRO GLY CYS GLN ASN
SEQRES 24 A 476 ASN SER LYS THR THR ILE ASP PRO PHE LEU ASP LEU SER
SEQRES 25 A 476 LEU ASP ILE LYS ASP LYS LYS LYS LEU TYR GLU CYS LEU
SEQRES 26 A 476 ASP SER PHE HIS LYS LYS GLU GLN LEU LYS ASP PHE ASN
SEQRES 27 A 476 TYR HIS CYS GLY GLU CYS ASN SER THR GLN ASP ALA ILE
SEQRES 28 A 476 LYS GLN LEU GLY ILE HIS LYS LEU PRO SER VAL LEU VAL
SEQRES 29 A 476 LEU GLN LEU LYS ARG PHE GLU HIS LEU LEU ASN GLY SER
SEQRES 30 A 476 ASN ARG LYS LEU ASP ASP PHE ILE GLU PHE PRO THR TYR
SEQRES 31 A 476 LEU ASN MET LYS ASN TYR CYS SER THR LYS GLU LYS ASP
SEQRES 32 A 476 LYS HIS SER GLU ASN GLY LYS VAL PRO ASP ILE ILE TYR
SEQRES 33 A 476 GLU LEU ILE GLY ILE VAL SER HIS LYS GLY THR VAL ASN
SEQRES 34 A 476 GLU GLY HIS TYR ILE ALA PHE CYS LYS ILE SER GLY GLY
SEQRES 35 A 476 GLN TRP PHE LYS PHE ASN ASP SER MET VAL SER SER ILE
SEQRES 36 A 476 SER GLN GLU GLU VAL LEU LYS GLU GLN ALA TYR LEU LEU
SEQRES 37 A 476 PHE TYR THR ILE ARG GLN VAL ASN
SEQRES 1 B 96 MET THR MET ASP THR ALA GLN LEU LYS SER GLN ILE GLN
SEQRES 2 B 96 GLN TYR LEU VAL GLU SER GLY ASN TYR GLU LEU ILE SER
SEQRES 3 B 96 ASN GLU LEU LYS ALA ARG LEU LEU GLN GLU GLY TRP VAL
SEQRES 4 B 96 ASP LYS VAL LYS ASP LEU THR LYS SER GLU MET ASN ILE
SEQRES 5 B 96 ASN GLU SER THR ASN PHE THR GLN ILE LEU SER THR VAL
SEQRES 6 B 96 GLU PRO LYS ALA LEU GLU MET VAL SER ASP SER THR ARG
SEQRES 7 B 96 GLU THR VAL LEU LYS GLN ILE ARG GLU PHE LEU GLU GLU
SEQRES 8 B 96 ILE VAL ASP THR GLN
SEQRES 1 C 99 MET THR GLU GLU THR ILE THR ILE ASP SER ILE SER ASN
SEQRES 2 C 99 GLY ILE LEU ASN ASN LEU LEU THR THR LEU ILE GLN ASP
SEQRES 3 C 99 ILE VAL ALA ARG GLU THR THR GLN GLN GLN LEU LEU LYS
SEQRES 4 C 99 THR ARG TYR PRO ASP LEU ARG SER TYR TYR PHE ASP PRO
SEQRES 5 C 99 ASN GLY SER LEU ASP ILE ASN GLY LEU GLN LYS GLN GLN
SEQRES 6 C 99 GLU SER SER GLN TYR ILE HIS CYS GLU ASN CYS GLY ARG
SEQRES 7 C 99 ASP VAL SER ALA ASN ARG LEU ALA ALA HIS LEU GLN ARG
SEQRES 8 C 99 CYS LEU SER ARG GLY ALA ARG ARG
SEQRES 1 D 96 MET ARG SER GLY ASP ALA GLU ILE LYS GLY ILE LYS PRO
SEQRES 2 D 96 LYS VAL ILE GLU GLU TYR SER LEU SER GLN GLY SER GLY
SEQRES 3 D 96 PRO SER ASN ASP SER TRP LYS SER LEU MET SER SER ALA
SEQRES 4 D 96 LYS ASP THR PRO LEU GLN TYR ASP HIS MET ASN ARG GLU
SEQRES 5 D 96 SER LEU LYS LYS TYR PHE ASN PRO ASN ALA GLN LEU ILE
SEQRES 6 D 96 GLU ASP PRO LEU ASP LYS PRO ILE GLN TYR ARG VAL CYS
SEQRES 7 D 96 GLU LYS CYS GLY LYS PRO LEU ALA LEU THR ALA ILE VAL
SEQRES 8 D 96 ASP HIS LEU GLU ASN
SEQRES 1 E 476 GLY ALA ALA ALA ALA MET SER ILE CYS PRO HIS ILE GLN
SEQRES 2 E 476 GLN VAL PHE GLN ASN GLU LYS SER LYS ASP GLY VAL LEU
SEQRES 3 E 476 LYS THR CYS ASN ALA ALA ARG TYR ILE LEU ASN HIS SER
SEQRES 4 E 476 VAL PRO LYS GLU LYS PHE LEU ASN THR MET LYS CYS GLY
SEQRES 5 E 476 THR CYS HIS GLU ILE ASN SER GLY ALA THR PHE MET CYS
SEQRES 6 E 476 LEU GLN CYS GLY PHE CYS GLY CYS TRP ASN HIS SER HIS
SEQRES 7 E 476 PHE LEU SER HIS SER LYS GLN ILE GLY HIS ILE PHE GLY
SEQRES 8 E 476 ILE ASN SER ASN ASN GLY LEU LEU PHE CYS PHE LYS CYS
SEQRES 9 E 476 GLU ASP TYR ILE GLY ASN ILE ASP LEU ILE ASN ASP ALA
SEQRES 10 E 476 ILE LEU ALA LYS TYR TRP ASP ASP VAL CYS THR LYS THR
SEQRES 11 E 476 MET VAL PRO SER MET GLU ARG ARG ASP GLY LEU SER GLY
SEQRES 12 E 476 LEU ILE ASN MET GLY SER THR CYS PHE MET SER SER ILE
SEQRES 13 E 476 LEU GLN CYS LEU ILE HIS ASN PRO TYR PHE ILE ARG HIS
SEQRES 14 E 476 SER MET SER GLN ILE HIS SER ASN ASN CYS LYS VAL ARG
SEQRES 15 E 476 SER PRO ASP LYS CYS PHE SER CYS ALA LEU ASP LYS ILE
SEQRES 16 E 476 VAL HIS GLU LEU TYR GLY ALA LEU ASN THR LYS GLN ALA
SEQRES 17 E 476 SER SER SER SER THR SER THR ASN ARG GLN THR GLY PHE
SEQRES 18 E 476 ILE TYR LEU LEU THR CYS ALA TRP LYS ILE ASN GLN ASN
SEQRES 19 E 476 LEU ALA GLY TYR SER GLN GLN ASP ALA HIS GLU PHE TRP
SEQRES 20 E 476 GLN PHE ILE ILE ASN GLN ILE HIS GLN SER TYR VAL LEU
SEQRES 21 E 476 ASP LEU PRO ASN ALA LYS GLU VAL SER ARG ALA ASN ASN
SEQRES 22 E 476 LYS GLN CYS GLU CYS ILE VAL HIS THR VAL PHE GLU GLY
SEQRES 23 E 476 SER LEU GLU SER SER ILE VAL CYS PRO GLY CYS GLN ASN
SEQRES 24 E 476 ASN SER LYS THR THR ILE ASP PRO PHE LEU ASP LEU SER
SEQRES 25 E 476 LEU ASP ILE LYS ASP LYS LYS LYS LEU TYR GLU CYS LEU
SEQRES 26 E 476 ASP SER PHE HIS LYS LYS GLU GLN LEU LYS ASP PHE ASN
SEQRES 27 E 476 TYR HIS CYS GLY GLU CYS ASN SER THR GLN ASP ALA ILE
SEQRES 28 E 476 LYS GLN LEU GLY ILE HIS LYS LEU PRO SER VAL LEU VAL
SEQRES 29 E 476 LEU GLN LEU LYS ARG PHE GLU HIS LEU LEU ASN GLY SER
SEQRES 30 E 476 ASN ARG LYS LEU ASP ASP PHE ILE GLU PHE PRO THR TYR
SEQRES 31 E 476 LEU ASN MET LYS ASN TYR CYS SER THR LYS GLU LYS ASP
SEQRES 32 E 476 LYS HIS SER GLU ASN GLY LYS VAL PRO ASP ILE ILE TYR
SEQRES 33 E 476 GLU LEU ILE GLY ILE VAL SER HIS LYS GLY THR VAL ASN
SEQRES 34 E 476 GLU GLY HIS TYR ILE ALA PHE CYS LYS ILE SER GLY GLY
SEQRES 35 E 476 GLN TRP PHE LYS PHE ASN ASP SER MET VAL SER SER ILE
SEQRES 36 E 476 SER GLN GLU GLU VAL LEU LYS GLU GLN ALA TYR LEU LEU
SEQRES 37 E 476 PHE TYR THR ILE ARG GLN VAL ASN
SEQRES 1 F 96 MET THR MET ASP THR ALA GLN LEU LYS SER GLN ILE GLN
SEQRES 2 F 96 GLN TYR LEU VAL GLU SER GLY ASN TYR GLU LEU ILE SER
SEQRES 3 F 96 ASN GLU LEU LYS ALA ARG LEU LEU GLN GLU GLY TRP VAL
SEQRES 4 F 96 ASP LYS VAL LYS ASP LEU THR LYS SER GLU MET ASN ILE
SEQRES 5 F 96 ASN GLU SER THR ASN PHE THR GLN ILE LEU SER THR VAL
SEQRES 6 F 96 GLU PRO LYS ALA LEU GLU MET VAL SER ASP SER THR ARG
SEQRES 7 F 96 GLU THR VAL LEU LYS GLN ILE ARG GLU PHE LEU GLU GLU
SEQRES 8 F 96 ILE VAL ASP THR GLN
SEQRES 1 G 99 MET THR GLU GLU THR ILE THR ILE ASP SER ILE SER ASN
SEQRES 2 G 99 GLY ILE LEU ASN ASN LEU LEU THR THR LEU ILE GLN ASP
SEQRES 3 G 99 ILE VAL ALA ARG GLU THR THR GLN GLN GLN LEU LEU LYS
SEQRES 4 G 99 THR ARG TYR PRO ASP LEU ARG SER TYR TYR PHE ASP PRO
SEQRES 5 G 99 ASN GLY SER LEU ASP ILE ASN GLY LEU GLN LYS GLN GLN
SEQRES 6 G 99 GLU SER SER GLN TYR ILE HIS CYS GLU ASN CYS GLY ARG
SEQRES 7 G 99 ASP VAL SER ALA ASN ARG LEU ALA ALA HIS LEU GLN ARG
SEQRES 8 G 99 CYS LEU SER ARG GLY ALA ARG ARG
SEQRES 1 H 96 MET ARG SER GLY ASP ALA GLU ILE LYS GLY ILE LYS PRO
SEQRES 2 H 96 LYS VAL ILE GLU GLU TYR SER LEU SER GLN GLY SER GLY
SEQRES 3 H 96 PRO SER ASN ASP SER TRP LYS SER LEU MET SER SER ALA
SEQRES 4 H 96 LYS ASP THR PRO LEU GLN TYR ASP HIS MET ASN ARG GLU
SEQRES 5 H 96 SER LEU LYS LYS TYR PHE ASN PRO ASN ALA GLN LEU ILE
SEQRES 6 H 96 GLU ASP PRO LEU ASP LYS PRO ILE GLN TYR ARG VAL CYS
SEQRES 7 H 96 GLU LYS CYS GLY LYS PRO LEU ALA LEU THR ALA ILE VAL
SEQRES 8 H 96 ASP HIS LEU GLU ASN
HET ZN A 501 1
HET ZN A 502 1
HET ZN A 503 1
HET ZN A 504 1
HET ZN A 505 1
HET ZN A 506 1
HET GOL A 507 6
HET ZN D 101 1
HET ZN E 501 1
HET ZN E 502 1
HET ZN E 503 1
HET ZN E 504 1
HET ZN E 505 1
HET ZN E 506 1
HET ZN H 101 1
HETNAM ZN ZINC ION
HETNAM GOL GLYCEROL
HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL
FORMUL 9 ZN 14(ZN 2+)
FORMUL 15 GOL C3 H8 O3
FORMUL 24 HOH *46(H2 O)
HELIX 1 1 CYS A 4 PHE A 11 1 8
HELIX 2 2 ASN A 13 HIS A 33 1 21
HELIX 3 3 VAL A 35 MET A 44 1 10
HELIX 4 4 SER A 72 GLY A 82 1 11
HELIX 5 5 ILE A 106 ASP A 111 1 6
HELIX 6 6 ALA A 112 LYS A 116 5 5
HELIX 7 7 TYR A 117 LYS A 124 1 8
HELIX 8 8 THR A 145 ILE A 156 1 12
HELIX 9 9 ASN A 158 SER A 167 1 10
HELIX 10 10 GLN A 168 CYS A 174 1 7
HELIX 11 11 CYS A 182 GLY A 196 1 15
HELIX 12 12 GLN A 213 ASN A 227 1 15
HELIX 13 13 ASP A 237 ASP A 256 1 20
HELIX 14 14 CYS A 273 PHE A 279 1 7
HELIX 15 15 LYS A 315 LYS A 325 1 11
HELIX 16 16 LYS A 389 CYS A 392 5 4
HELIX 17 17 SER A 451 LEU A 456 1 6
HELIX 18 18 GLN B 7 SER B 19 1 13
HELIX 19 19 GLY B 20 GLU B 36 1 17
HELIX 20 20 GLY B 37 ASN B 53 1 17
HELIX 21 21 ASN B 57 MET B 72 1 16
HELIX 22 22 SER B 74 ILE B 92 1 19
HELIX 23 23 THR C 7 TYR C 42 1 36
HELIX 24 24 LYS D 12 TYR D 19 1 8
HELIX 25 25 SER D 31 SER D 34 5 4
HELIX 26 26 LEU D 35 ASP D 41 1 7
HELIX 27 27 ASN D 50 PHE D 58 1 9
HELIX 28 28 LEU D 87 GLU D 95 1 9
HELIX 29 29 CYS E 4 ASN E 13 1 10
HELIX 30 30 ASN E 13 HIS E 33 1 21
HELIX 31 31 VAL E 35 THR E 43 1 9
HELIX 32 32 SER E 72 GLY E 82 1 11
HELIX 33 33 ILE E 106 ASP E 111 1 6
HELIX 34 34 ALA E 112 LYS E 116 5 5
HELIX 35 35 TYR E 117 LYS E 124 1 8
HELIX 36 36 THR E 145 ILE E 156 1 12
HELIX 37 37 ASN E 158 SER E 167 1 10
HELIX 38 38 CYS E 182 GLY E 196 1 15
HELIX 39 39 GLN E 213 ASN E 227 1 15
HELIX 40 40 ASP E 237 ASP E 256 1 20
HELIX 41 41 LYS E 315 HIS E 324 1 10
HELIX 42 42 LYS E 389 CYS E 392 5 4
HELIX 43 43 SER E 451 LEU E 456 1 6
HELIX 44 44 LYS F 9 SER F 19 1 11
HELIX 45 45 GLY F 20 GLY F 37 1 18
HELIX 46 46 GLY F 37 ASN F 53 1 17
HELIX 47 47 ASN F 57 VAL F 73 1 17
HELIX 48 48 SER F 74 VAL F 93 1 20
HELIX 49 49 THR G 7 TYR G 42 1 36
HELIX 50 50 LYS H 14 GLU H 18 5 5
HELIX 51 51 SER H 31 SER H 34 5 4
HELIX 52 52 LEU H 35 THR H 42 1 8
HELIX 53 53 ASN H 50 PHE H 58 1 9
HELIX 54 54 ALA H 89 LEU H 94 1 6
SHEET 1 A 5 CYS A 66 CYS A 68 0
SHEET 2 A 5 THR A 57 CYS A 60 -1 N PHE A 58 O GLY A 67
SHEET 3 A 5 PHE A 85 ASN A 88 -1 O ILE A 87 N MET A 59
SHEET 4 A 5 LEU A 94 CYS A 96 -1 O PHE A 95 N GLY A 86
SHEET 5 A 5 ASP A 101 TYR A 102 -1 O ASP A 101 N CYS A 96
SHEET 1 B 3 THR A 125 MET A 126 0
SHEET 2 B 3 TYR D 75 CYS D 78 -1 O VAL D 77 N MET A 126
SHEET 3 B 3 PRO D 84 ALA D 86 -1 O LEU D 85 N ARG D 76
SHEET 1 C 4 ASN A 295 PHE A 303 0
SHEET 2 C 4 GLY A 281 VAL A 288 -1 N LEU A 283 O ASP A 301
SHEET 3 C 4 ALA A 345 LYS A 353 -1 O ILE A 346 N VAL A 288
SHEET 4 C 4 GLU A 327 LEU A 329 -1 N GLU A 327 O LYS A 347
SHEET 1 D 5 LEU A 306 LEU A 308 0
SHEET 2 D 5 VAL A 357 LEU A 362 1 O GLN A 361 N LEU A 306
SHEET 3 D 5 ALA A 460 VAL A 470 -1 O LEU A 463 N LEU A 360
SHEET 4 D 5 ILE A 409 GLY A 421 -1 N ILE A 410 O GLN A 469
SHEET 5 D 5 TYR A 385 ASN A 387 -1 N LEU A 386 O TYR A 411
SHEET 1 E 7 LEU A 306 LEU A 308 0
SHEET 2 E 7 VAL A 357 LEU A 362 1 O GLN A 361 N LEU A 306
SHEET 3 E 7 ALA A 460 VAL A 470 -1 O LEU A 463 N LEU A 360
SHEET 4 E 7 ILE A 409 GLY A 421 -1 N ILE A 410 O GLN A 469
SHEET 5 E 7 GLY A 426 ILE A 434 -1 O HIS A 427 N LYS A 420
SHEET 6 E 7 GLN A 438 ASN A 443 -1 O PHE A 442 N ALA A 430
SHEET 7 E 7 MET A 446 ILE A 450 -1 O MET A 446 N ASN A 443
SHEET 1 F 2 PHE A 365 HIS A 367 0
SHEET 2 F 2 ASN A 373 LYS A 375 -1 O ARG A 374 N GLU A 366
SHEET 1 G 2 VAL B 93 THR B 95 0
SHEET 2 G 2 ILE D 8 ILE D 11 -1 O LYS D 9 N ASP B 94
SHEET 1 H 5 CYS E 66 CYS E 68 0
SHEET 2 H 5 THR E 57 CYS E 60 -1 N PHE E 58 O GLY E 67
SHEET 3 H 5 PHE E 85 ASN E 88 -1 O ILE E 87 N MET E 59
SHEET 4 H 5 LEU E 94 CYS E 96 -1 O PHE E 95 N GLY E 86
SHEET 5 H 5 ASP E 101 TYR E 102 -1 O ASP E 101 N CYS E 96
SHEET 1 I 3 THR E 125 MET E 126 0
SHEET 2 I 3 TYR H 75 CYS H 78 -1 O VAL H 77 N MET E 126
SHEET 3 I 3 PRO H 84 ALA H 86 -1 O LEU H 85 N ARG H 76
SHEET 1 J 4 ASN E 295 PHE E 303 0
SHEET 2 J 4 GLY E 281 VAL E 288 -1 N ILE E 287 O LYS E 297
SHEET 3 J 4 SER E 341 LYS E 353 -1 O GLY E 350 N GLU E 284
SHEET 4 J 4 LYS E 326 CYS E 336 -1 N CYS E 336 O SER E 341
SHEET 1 K 5 ASP E 305 ASP E 309 0
SHEET 2 K 5 VAL E 357 LYS E 363 1 O GLN E 361 N LEU E 306
SHEET 3 K 5 ALA E 460 VAL E 470 -1 O TYR E 461 N LEU E 362
SHEET 4 K 5 ILE E 409 LYS E 420 -1 N ILE E 414 O PHE E 464
SHEET 5 K 5 TYR E 385 ASN E 387 -1 N LEU E 386 O TYR E 411
SHEET 1 L 7 ASP E 305 ASP E 309 0
SHEET 2 L 7 VAL E 357 LYS E 363 1 O GLN E 361 N LEU E 306
SHEET 3 L 7 ALA E 460 VAL E 470 -1 O TYR E 461 N LEU E 362
SHEET 4 L 7 ILE E 409 LYS E 420 -1 N ILE E 414 O PHE E 464
SHEET 5 L 7 HIS E 427 LYS E 433 -1 O PHE E 431 N ILE E 416
SHEET 6 L 7 TRP E 439 ASN E 443 -1 O PHE E 442 N ALA E 430
SHEET 7 L 7 MET E 446 ILE E 450 -1 O MET E 446 N ASN E 443
LINK SG CYS A 4 ZN ZN A 501 1555 1555 1.97
LINK ND1 HIS A 6 ZN ZN A 501 1555 1555 2.04
LINK SG CYS A 46 ZN ZN A 502 1555 1555 2.36
LINK SG CYS A 49 ZN ZN A 502 1555 1555 2.38
LINK SG CYS A 60 ZN ZN A 503 1555 1555 2.25
LINK SG CYS A 63 ZN ZN A 503 1555 1555 2.22
LINK SG CYS A 68 ZN ZN A 502 1555 1555 2.16
LINK ND1 HIS A 73 ZN ZN A 502 1555 1555 1.79
LINK NE2 HIS A 77 ZN ZN A 503 1555 1555 1.75
LINK ND1 HIS A 83 ZN ZN A 503 1555 1555 2.08
LINK SG CYS A 96 ZN ZN A 501 1555 1555 2.21
LINK SG CYS A 99 ZN ZN A 501 1555 1555 2.17
LINK NE2 HIS A 170 ZN ZN A 504 1555 1555 2.52
LINK SG CYS A 174 ZN ZN A 504 1555 1555 2.46
LINK SG CYS A 182 ZN ZN A 504 1555 1555 2.66
LINK SG CYS A 185 ZN ZN A 504 1555 1555 2.24
LINK SG CYS A 271 ZN ZN A 505 1555 1555 2.23
LINK SG CYS A 273 ZN ZN A 505 1555 1555 2.27
LINK ND1 HIS A 276 ZN ZN A 505 1555 1555 2.21
LINK SG CYS A 289 ZN ZN A 506 1555 1555 2.84
LINK SG CYS A 336 ZN ZN A 506 1555 1555 2.51
LINK SG CYS D 78 ZN ZN D 101 1555 1555 2.22
LINK SG CYS D 81 ZN ZN D 101 1555 1555 2.24
LINK NE2 HIS D 93 ZN ZN D 101 1555 1555 2.07
LINK ZN ZN D 101 O HOH D 203 1555 1555 2.38
LINK SG CYS E 4 ZN ZN E 501 1555 1555 2.05
LINK ND1 HIS E 6 ZN ZN E 501 1555 1555 2.32
LINK SG CYS E 46 ZN ZN E 502 1555 1555 2.51
LINK SG CYS E 60 ZN ZN E 503 1555 1555 2.22
LINK SG CYS E 63 ZN ZN E 503 1555 1555 2.08
LINK SG CYS E 68 ZN ZN E 502 1555 1555 2.14
LINK ND1 HIS E 73 ZN ZN E 502 1555 1555 2.07
LINK NE2 HIS E 77 ZN ZN E 503 1555 1555 2.07
LINK ND1 HIS E 83 ZN ZN E 503 1555 1555 2.03
LINK SG CYS E 96 ZN ZN E 501 1555 1555 2.58
LINK SG CYS E 99 ZN ZN E 501 1555 1555 2.12
LINK SG CYS E 174 ZN ZN E 504 1555 1555 2.12
LINK SG CYS E 182 ZN ZN E 504 1555 1555 2.09
LINK SG CYS E 185 ZN ZN E 504 1555 1555 2.28
LINK SG CYS E 271 ZN ZN E 505 1555 1555 2.03
LINK SG CYS E 273 ZN ZN E 505 1555 1555 2.30
LINK ND1 HIS E 276 ZN ZN E 505 1555 1555 1.97
LINK SG CYS E 289 ZN ZN E 506 1555 1555 2.10
LINK SG CYS E 292 ZN ZN E 506 1555 1555 2.31
LINK SG CYS E 336 ZN ZN E 506 1555 1555 2.29
LINK SG CYS E 339 ZN ZN E 506 1555 1555 2.25
LINK SG CYS H 78 ZN ZN H 101 1555 1555 2.25
LINK SG CYS H 81 ZN ZN H 101 1555 1555 2.01
CISPEP 1 GLN A 228 ASN A 229 0 -15.06
CISPEP 2 LEU A 230 ALA A 231 0 2.30
CISPEP 3 ALA A 231 GLY A 232 0 6.12
CISPEP 4 ALA A 266 ASN A 267 0 8.40
CISPEP 5 ASN A 268 LYS A 269 0 28.30
CISPEP 6 THR B 5 ALA B 6 0 3.68
CISPEP 7 PRO D 27 SER D 28 0 -17.19
CISPEP 8 GLN E 228 ASN E 229 0 6.25
CISPEP 9 LEU E 230 ALA E 231 0 -4.99
CISPEP 10 ALA E 231 GLY E 232 0 -21.62
CISPEP 11 SER E 234 GLN E 235 0 -17.27
SITE 1 AC1 4 CYS A 4 HIS A 6 CYS A 96 CYS A 99
SITE 1 AC2 4 CYS A 46 CYS A 49 CYS A 68 HIS A 73
SITE 1 AC3 4 CYS A 60 CYS A 63 HIS A 77 HIS A 83
SITE 1 AC4 4 HIS A 170 CYS A 174 CYS A 182 CYS A 185
SITE 1 AC5 4 HIS A 250 CYS A 271 CYS A 273 HIS A 276
SITE 1 AC6 5 CYS A 289 CYS A 292 CYS A 336 CYS A 339
SITE 2 AC6 5 ASN A 340
SITE 1 AC7 5 ARG A 468 GLN A 469 LEU G 23 HIS H 48
SITE 2 AC7 5 ASP H 67
SITE 1 AC8 4 CYS D 78 CYS D 81 HIS D 93 HOH D 203
SITE 1 AC9 4 CYS E 4 HIS E 6 CYS E 96 CYS E 99
SITE 1 BC1 4 CYS E 46 CYS E 49 CYS E 68 HIS E 73
SITE 1 BC2 4 CYS E 60 CYS E 63 HIS E 77 HIS E 83
SITE 1 BC3 4 HIS E 170 CYS E 174 CYS E 182 CYS E 185
SITE 1 BC4 4 HIS E 250 CYS E 271 CYS E 273 HIS E 276
SITE 1 BC5 4 CYS E 289 CYS E 292 CYS E 336 CYS E 339
SITE 1 BC6 4 CYS H 78 CYS H 81 HIS H 93 HOH H 202
CRYST1 76.490 79.202 265.943 90.00 90.00 90.00 P 21 21 21 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 0.013074 0.000000 0.000000 0.00000
SCALE2 0.000000 0.012626 0.000000 0.00000
SCALE3 0.000000 0.000000 0.003760 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
