HEADER HYDROLASE 30-JUL-09 3IHP
TITLE COVALENT UBIQUITIN-USP5 COMPLEX
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: UBIQUITIN CARBOXYL-TERMINAL HYDROLASE 5;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: UBIQUITIN THIOESTERASE 5, UBIQUITIN-SPECIFIC-PROCESSING
COMPND 5 PROTEASE 5, DEUBIQUITINATING ENZYME 5, ISOPEPTIDASE T;
COMPND 6 EC: 3.1.2.15;
COMPND 7 ENGINEERED: YES;
COMPND 8 MOL_ID: 2;
COMPND 9 MOLECULE: UBIQUITIN;
COMPND 10 CHAIN: C, D;
COMPND 11 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: ISOT, USP5;
SOURCE 6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 8 EXPRESSION_SYSTEM_STRAIN: BL21 (DE3);
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PET28A-LIC;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 GENE: RPS27A, UBA52, UBA80, UBB, UBC, UBCEP1, UBCEP2;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: B21 (DE3);
SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PTBY2
KEYWDS HYDROLASE, PROTEASE, THIOL PROTEASE, UBL CONJUGATION PATHWAY, METAL-
KEYWDS 2 BINDING, ZINC-FINGER, STRUCTURAL GENOMICS, STRUCTURAL GENOMICS
KEYWDS 3 CONSORTIUM, SGC, ACETYLATION, ALTERNATIVE SPLICING, PHOSPHOPROTEIN,
KEYWDS 4 ZINC, CYTOPLASM, ISOPEPTIDE BOND, NUCLEUS, UBL CONJUGATION
EXPDTA X-RAY DIFFRACTION
AUTHOR J.R.WALKER,G.V.AVVAKUMOV,S.XUE,C.BUTLER-COLE,J.WEIGELT,C.BOUNTRA,
AUTHOR 2 C.H.ARROWSMITH,A.M.EDWARDS,A.BOCHKAREV,S.DHE-PAGANON,STRUCTURAL
AUTHOR 3 GENOMICS CONSORTIUM (SGC)
REVDAT 2 06-SEP-23 3IHP 1 REMARK SEQADV LINK
REVDAT 1 29-DEC-09 3IHP 0
JRNL AUTH J.R.WALKER,G.V.AVVAKUMOV,S.XUE,C.BUTLER-COLE,J.WEIGELT,
JRNL AUTH 2 C.BOUNTRA,C.H.ARROWSMITH,A.M.EDWARDS,A.BOCHKAREV,
JRNL AUTH 3 S.DHE-PAGANON
JRNL TITL COVALENT UBIQUITIN-USP5 COMPLEX
JRNL REF TO BE PUBLISHED
JRNL REFN
REMARK 2
REMARK 2 RESOLUTION. 2.80 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.5.0102
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) : 2.80
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 34.90
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 98.1
REMARK 3 NUMBER OF REFLECTIONS : 62592
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) : 0.227
REMARK 3 R VALUE (WORKING SET) : 0.224
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 : 3298
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) : 2.80
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 2.87
REMARK 3 REFLECTION IN BIN (WORKING SET) : 4388
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 94.21
REMARK 3 BIN R VALUE (WORKING SET) : 0.3030
REMARK 3 BIN FREE R VALUE SET COUNT : 234
REMARK 3 BIN FREE R VALUE : 0.3580
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 11733
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 9
REMARK 3 SOLVENT ATOMS : 32
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 73.95
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -0.35000
REMARK 3 B22 (A**2) : 0.39000
REMARK 3 B33 (A**2) : -0.04000
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): 0.563
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.343
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.272
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 30.552
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.926
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.889
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 12019 ; 0.011 ; 0.022
REMARK 3 BOND LENGTHS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 16278 ; 1.308 ; 1.967
REMARK 3 BOND ANGLES OTHERS (DEGREES): NULL ; NULL ; NULL
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 1491 ; 5.975 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 557 ;36.014 ;24.560
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 2014 ;19.655 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 68 ;19.923 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1803 ; 0.090 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 9149 ; 0.005 ; 0.021
REMARK 3 GENERAL PLANES OTHERS (A): NULL ; NULL ; NULL
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): 7512 ; 0.469 ; 1.500
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 12082 ; 0.898 ; 2.000
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 4507 ; 1.275 ; 3.000
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 4196 ; 2.237 ; 4.500
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 : 2
REMARK 3
REMARK 3 NCS GROUP NUMBER : 1
REMARK 3 CHAIN NAMES : A B
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 A 1 A 835 4
REMARK 3 1 B 1 B 835 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 1 A (A): 4816 ; 0.61 ; 0.50
REMARK 3 MEDIUM THERMAL 1 A (A**2): 4816 ; 0.39 ; 2.00
REMARK 3
REMARK 3 NCS GROUP NUMBER : 2
REMARK 3 CHAIN NAMES : C D
REMARK 3 NUMBER OF COMPONENTS NCS GROUP : 1
REMARK 3 COMPONENT C SSSEQI TO C SSSEQI CODE
REMARK 3 1 C 1 C 76 4
REMARK 3 1 D 1 D 76 4
REMARK 3 GROUP CHAIN COUNT RMS WEIGHT
REMARK 3 MEDIUM POSITIONAL 2 C (A): 600 ; 0.33 ; 0.50
REMARK 3 MEDIUM THERMAL 2 C (A**2): 600 ; 0.45 ; 2.00
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 26
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 1 A 121
REMARK 3 ORIGIN FOR THE GROUP (A): -77.4876 -62.8490 -74.8262
REMARK 3 T TENSOR
REMARK 3 T11: 0.4747 T22: 0.2297
REMARK 3 T33: 0.1774 T12: -0.1132
REMARK 3 T13: 0.0158 T23: -0.0581
REMARK 3 L TENSOR
REMARK 3 L11: 5.5849 L22: 0.4602
REMARK 3 L33: 5.1070 L12: -0.6566
REMARK 3 L13: 2.5799 L23: 0.3002
REMARK 3 S TENSOR
REMARK 3 S11: 0.1846 S12: -0.1417 S13: -0.0265
REMARK 3 S21: -0.0853 S22: 0.0434 S23: -0.0661
REMARK 3 S31: 0.3311 S32: 0.0756 S33: -0.2280
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 : A 122 A 203
REMARK 3 ORIGIN FOR THE GROUP (A): -59.4187 -53.9060 -79.8348
REMARK 3 T TENSOR
REMARK 3 T11: 0.5287 T22: 0.2683
REMARK 3 T33: 0.1994 T12: -0.0478
REMARK 3 T13: 0.0467 T23: 0.0421
REMARK 3 L TENSOR
REMARK 3 L11: 4.2954 L22: 0.6072
REMARK 3 L33: 0.2654 L12: 1.3205
REMARK 3 L13: 0.4169 L23: 0.3157
REMARK 3 S TENSOR
REMARK 3 S11: 0.1766 S12: -0.1414 S13: -0.0786
REMARK 3 S21: -0.0657 S22: -0.1829 S23: -0.0742
REMARK 3 S31: 0.0911 S32: -0.0369 S33: 0.0063
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 : A 204 A 282
REMARK 3 ORIGIN FOR THE GROUP (A): -37.1802 -45.4550 -76.4435
REMARK 3 T TENSOR
REMARK 3 T11: 0.3187 T22: 0.2189
REMARK 3 T33: 0.3092 T12: -0.0331
REMARK 3 T13: 0.1212 T23: 0.0980
REMARK 3 L TENSOR
REMARK 3 L11: 4.4352 L22: 4.7357
REMARK 3 L33: 5.4002 L12: -0.8951
REMARK 3 L13: -0.2906 L23: 1.2620
REMARK 3 S TENSOR
REMARK 3 S11: -0.0974 S12: -0.1568 S13: -0.1709
REMARK 3 S21: 0.2175 S22: 0.1597 S23: 0.5948
REMARK 3 S31: 0.0747 S32: -0.4805 S33: -0.0622
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 : A 283 A 462
REMARK 3 ORIGIN FOR THE GROUP (A): -61.6675 -61.6046 -53.8172
REMARK 3 T TENSOR
REMARK 3 T11: 0.3838 T22: 0.3538
REMARK 3 T33: 0.2193 T12: -0.0669
REMARK 3 T13: 0.0342 T23: -0.0833
REMARK 3 L TENSOR
REMARK 3 L11: 2.6241 L22: 0.8334
REMARK 3 L33: 2.5411 L12: -0.1481
REMARK 3 L13: 0.5550 L23: 0.3664
REMARK 3 S TENSOR
REMARK 3 S11: 0.0788 S12: 0.1261 S13: 0.0041
REMARK 3 S21: -0.2290 S22: -0.1753 S23: 0.0269
REMARK 3 S31: 0.1955 S32: -0.2748 S33: 0.0965
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 : A 463 A 513
REMARK 3 ORIGIN FOR THE GROUP (A): -40.4289 -53.4996 -32.8220
REMARK 3 T TENSOR
REMARK 3 T11: 0.3537 T22: 0.4969
REMARK 3 T33: 0.3658 T12: -0.0529
REMARK 3 T13: -0.0176 T23: 0.1021
REMARK 3 L TENSOR
REMARK 3 L11: 0.3761 L22: 1.1413
REMARK 3 L33: 1.8699 L12: -0.5527
REMARK 3 L13: -0.7858 L23: 1.6218
REMARK 3 S TENSOR
REMARK 3 S11: -0.0119 S12: -0.2041 S13: 0.1988
REMARK 3 S21: 0.1412 S22: 0.0937 S23: -0.1404
REMARK 3 S31: 0.0364 S32: 0.3127 S33: -0.0819
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 : A 514 A 607
REMARK 3 ORIGIN FOR THE GROUP (A): -41.7260 -54.8597 -34.0322
REMARK 3 T TENSOR
REMARK 3 T11: 0.3258 T22: 0.3613
REMARK 3 T33: 0.3200 T12: -0.0573
REMARK 3 T13: 0.0539 T23: -0.0133
REMARK 3 L TENSOR
REMARK 3 L11: 0.4945 L22: 0.5731
REMARK 3 L33: 1.1792 L12: 0.0471
REMARK 3 L13: 0.1752 L23: 0.5755
REMARK 3 S TENSOR
REMARK 3 S11: 0.0034 S12: -0.0387 S13: -0.0145
REMARK 3 S21: 0.0125 S22: 0.0218 S23: -0.1226
REMARK 3 S31: 0.0585 S32: 0.2655 S33: -0.0252
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 : A 608 A 711
REMARK 3 ORIGIN FOR THE GROUP (A): -61.4187 -26.1704 -21.0356
REMARK 3 T TENSOR
REMARK 3 T11: 0.2858 T22: 0.5360
REMARK 3 T33: 0.4833 T12: 0.0941
REMARK 3 T13: -0.1429 T23: -0.1801
REMARK 3 L TENSOR
REMARK 3 L11: 0.2372 L22: 2.1599
REMARK 3 L33: 1.3521 L12: 0.5381
REMARK 3 L13: 0.0436 L23: 1.9370
REMARK 3 S TENSOR
REMARK 3 S11: 0.0026 S12: 0.0682 S13: 0.2018
REMARK 3 S21: -0.2921 S22: -0.5251 S23: 0.6153
REMARK 3 S31: -0.2877 S32: -0.5922 S33: 0.5224
REMARK 3
REMARK 3 TLS GROUP : 8
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 712 A 749
REMARK 3 ORIGIN FOR THE GROUP (A): -73.7781 -42.7836 -37.4903
REMARK 3 T TENSOR
REMARK 3 T11: 0.1787 T22: 0.4626
REMARK 3 T33: 0.2691 T12: 0.0385
REMARK 3 T13: -0.0245 T23: -0.1675
REMARK 3 L TENSOR
REMARK 3 L11: 9.6693 L22: 5.8601
REMARK 3 L33: 3.2299 L12: 1.8553
REMARK 3 L13: -2.5012 L23: -0.2442
REMARK 3 S TENSOR
REMARK 3 S11: 0.1754 S12: -0.0119 S13: 0.2874
REMARK 3 S21: 0.2337 S22: -0.3315 S23: 0.2319
REMARK 3 S31: -0.4319 S32: -0.5352 S33: 0.1561
REMARK 3
REMARK 3 TLS GROUP : 9
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : A 769 A 834
REMARK 3 ORIGIN FOR THE GROUP (A): -48.1201 -68.0426 -46.2916
REMARK 3 T TENSOR
REMARK 3 T11: 0.4023 T22: 0.2688
REMARK 3 T33: 0.3320 T12: 0.0062
REMARK 3 T13: 0.0952 T23: -0.0304
REMARK 3 L TENSOR
REMARK 3 L11: 2.1711 L22: 1.0135
REMARK 3 L33: 3.8495 L12: 0.5145
REMARK 3 L13: -1.2646 L23: 0.6825
REMARK 3 S TENSOR
REMARK 3 S11: -0.0352 S12: 0.2057 S13: -0.2945
REMARK 3 S21: -0.0164 S22: -0.0001 S23: -0.0826
REMARK 3 S31: 0.5683 S32: 0.1752 S33: 0.0354
REMARK 3
REMARK 3 TLS GROUP : 10
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 1 B 40
REMARK 3 ORIGIN FOR THE GROUP (A): -74.1873 20.2458 13.9830
REMARK 3 T TENSOR
REMARK 3 T11: 0.3700 T22: 0.1965
REMARK 3 T33: 0.2209 T12: 0.0069
REMARK 3 T13: -0.0564 T23: -0.0537
REMARK 3 L TENSOR
REMARK 3 L11: 3.9071 L22: 6.4874
REMARK 3 L33: 0.8984 L12: 2.4008
REMARK 3 L13: -1.8658 L23: -0.0893
REMARK 3 S TENSOR
REMARK 3 S11: 0.0427 S12: -0.0949 S13: 0.1780
REMARK 3 S21: 0.1649 S22: -0.0288 S23: 0.1385
REMARK 3 S31: 0.0793 S32: 0.0285 S33: -0.0139
REMARK 3
REMARK 3 TLS GROUP : 11
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 41 B 156
REMARK 3 ORIGIN FOR THE GROUP (A): -73.5557 22.5945 15.7112
REMARK 3 T TENSOR
REMARK 3 T11: 0.3872 T22: 0.1962
REMARK 3 T33: 0.2305 T12: -0.0241
REMARK 3 T13: -0.0467 T23: -0.1099
REMARK 3 L TENSOR
REMARK 3 L11: 2.7396 L22: 5.2606
REMARK 3 L33: 2.3924 L12: 1.2209
REMARK 3 L13: 0.0222 L23: 0.3850
REMARK 3 S TENSOR
REMARK 3 S11: 0.2554 S12: -0.1025 S13: 0.0076
REMARK 3 S21: 0.1474 S22: -0.3272 S23: 0.1233
REMARK 3 S31: -0.1564 S32: -0.0087 S33: 0.0718
REMARK 3
REMARK 3 TLS GROUP : 12
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 173 B 320
REMARK 3 ORIGIN FOR THE GROUP (A):-117.3690 19.5143 -0.5808
REMARK 3 T TENSOR
REMARK 3 T11: 0.4088 T22: 0.4445
REMARK 3 T33: 0.3134 T12: 0.2114
REMARK 3 T13: 0.0653 T23: 0.1618
REMARK 3 L TENSOR
REMARK 3 L11: 0.1516 L22: 4.8296
REMARK 3 L33: 5.9137 L12: -0.8543
REMARK 3 L13: 0.6750 L23: -2.2633
REMARK 3 S TENSOR
REMARK 3 S11: 0.0053 S12: -0.0634 S13: 0.0377
REMARK 3 S21: -0.3756 S22: -0.3726 S23: -0.4398
REMARK 3 S31: 0.7013 S32: 0.9586 S33: 0.3673
REMARK 3
REMARK 3 TLS GROUP : 13
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 321 B 462
REMARK 3 ORIGIN FOR THE GROUP (A): -90.2280 -2.3582 12.5205
REMARK 3 T TENSOR
REMARK 3 T11: 0.3464 T22: 0.1949
REMARK 3 T33: 0.2979 T12: -0.0033
REMARK 3 T13: -0.0210 T23: -0.0698
REMARK 3 L TENSOR
REMARK 3 L11: 2.3189 L22: 1.9626
REMARK 3 L33: 1.4790 L12: 0.9480
REMARK 3 L13: -0.2328 L23: 0.6572
REMARK 3 S TENSOR
REMARK 3 S11: 0.1141 S12: -0.0074 S13: -0.0184
REMARK 3 S21: 0.0131 S22: 0.0908 S23: -0.1783
REMARK 3 S31: -0.2111 S32: 0.1201 S33: -0.2049
REMARK 3
REMARK 3 TLS GROUP : 14
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 463 B 520
REMARK 3 ORIGIN FOR THE GROUP (A):-114.7891 -19.4106 3.2659
REMARK 3 T TENSOR
REMARK 3 T11: 0.3380 T22: 0.2726
REMARK 3 T33: 0.4306 T12: -0.0196
REMARK 3 T13: -0.0889 T23: 0.0168
REMARK 3 L TENSOR
REMARK 3 L11: 0.6138 L22: 1.0368
REMARK 3 L33: 1.1945 L12: -0.4922
REMARK 3 L13: -0.6461 L23: 1.1194
REMARK 3 S TENSOR
REMARK 3 S11: -0.0156 S12: 0.1181 S13: -0.2929
REMARK 3 S21: -0.0505 S22: -0.1055 S23: 0.2269
REMARK 3 S31: 0.0951 S32: -0.1762 S33: 0.1210
REMARK 3
REMARK 3 TLS GROUP : 15
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 521 B 607
REMARK 3 ORIGIN FOR THE GROUP (A):-108.8940 -23.0210 3.7434
REMARK 3 T TENSOR
REMARK 3 T11: 0.2955 T22: 0.2491
REMARK 3 T33: 0.3523 T12: 0.0278
REMARK 3 T13: -0.0690 T23: 0.0128
REMARK 3 L TENSOR
REMARK 3 L11: 0.8409 L22: 0.6114
REMARK 3 L33: 1.2446 L12: 0.3744
REMARK 3 L13: 0.0505 L23: 0.6223
REMARK 3 S TENSOR
REMARK 3 S11: -0.0084 S12: -0.0058 S13: -0.1378
REMARK 3 S21: 0.0545 S22: -0.0039 S23: 0.1079
REMARK 3 S31: 0.0851 S32: -0.1511 S33: 0.0122
REMARK 3
REMARK 3 TLS GROUP : 16
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 608 B 712
REMARK 3 ORIGIN FOR THE GROUP (A): -90.9323 -30.4362 -26.2722
REMARK 3 T TENSOR
REMARK 3 T11: 0.2337 T22: 0.4960
REMARK 3 T33: 0.5427 T12: -0.1419
REMARK 3 T13: 0.0803 T23: -0.1851
REMARK 3 L TENSOR
REMARK 3 L11: 0.2444 L22: 0.9533
REMARK 3 L33: 4.5937 L12: -0.0035
REMARK 3 L13: 0.3445 L23: 2.2384
REMARK 3 S TENSOR
REMARK 3 S11: -0.0093 S12: 0.1990 S13: 0.1129
REMARK 3 S21: -0.1889 S22: 0.3899 S23: -0.3216
REMARK 3 S31: -0.2287 S32: 0.6045 S33: -0.3806
REMARK 3
REMARK 3 TLS GROUP : 17
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 713 B 750
REMARK 3 ORIGIN FOR THE GROUP (A): -79.0098 -15.7455 -8.0439
REMARK 3 T TENSOR
REMARK 3 T11: 0.1296 T22: 0.3811
REMARK 3 T33: 0.3502 T12: -0.0657
REMARK 3 T13: 0.0375 T23: -0.2378
REMARK 3 L TENSOR
REMARK 3 L11: 12.6904 L22: 4.4180
REMARK 3 L33: 9.1787 L12: -4.5425
REMARK 3 L13: -0.2663 L23: -0.2535
REMARK 3 S TENSOR
REMARK 3 S11: 0.1094 S12: -0.1475 S13: 0.1950
REMARK 3 S21: -0.5574 S22: 0.3835 S23: -0.4683
REMARK 3 S31: -0.2787 S32: 0.9051 S33: -0.4930
REMARK 3
REMARK 3 TLS GROUP : 18
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : B 768 B 835
REMARK 3 ORIGIN FOR THE GROUP (A):-103.8947 -10.9400 18.4682
REMARK 3 T TENSOR
REMARK 3 T11: 0.2948 T22: 0.2502
REMARK 3 T33: 0.2632 T12: 0.0481
REMARK 3 T13: -0.0213 T23: -0.0154
REMARK 3 L TENSOR
REMARK 3 L11: 2.1883 L22: 2.7664
REMARK 3 L33: 1.5954 L12: -0.2767
REMARK 3 L13: 0.5229 L23: 0.4103
REMARK 3 S TENSOR
REMARK 3 S11: 0.1133 S12: -0.1560 S13: 0.0165
REMARK 3 S21: 0.2408 S22: 0.0046 S23: 0.1281
REMARK 3 S31: -0.0337 S32: -0.0129 S33: -0.1179
REMARK 3
REMARK 3 TLS GROUP : 19
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 1 C 16
REMARK 3 ORIGIN FOR THE GROUP (A): -47.0098 -40.9947 -30.8543
REMARK 3 T TENSOR
REMARK 3 T11: 0.2448 T22: 0.3346
REMARK 3 T33: 0.3338 T12: -0.1347
REMARK 3 T13: -0.0263 T23: -0.1017
REMARK 3 L TENSOR
REMARK 3 L11: 8.9886 L22: 2.7594
REMARK 3 L33: 7.5587 L12: 2.6123
REMARK 3 L13: 0.2730 L23: -5.6127
REMARK 3 S TENSOR
REMARK 3 S11: -0.2569 S12: -0.0294 S13: 0.4714
REMARK 3 S21: 0.1498 S22: -0.1680 S23: -0.1987
REMARK 3 S31: -0.0977 S32: 0.3049 S33: 0.4249
REMARK 3
REMARK 3 TLS GROUP : 20
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 17 C 39
REMARK 3 ORIGIN FOR THE GROUP (A): -49.6866 -34.2992 -38.7771
REMARK 3 T TENSOR
REMARK 3 T11: 0.7129 T22: 0.2077
REMARK 3 T33: 0.4363 T12: -0.1242
REMARK 3 T13: 0.0993 T23: 0.0206
REMARK 3 L TENSOR
REMARK 3 L11: 15.1866 L22: 5.1020
REMARK 3 L33: 4.9508 L12: -2.1986
REMARK 3 L13: -5.4423 L23: 5.1709
REMARK 3 S TENSOR
REMARK 3 S11: 0.2687 S12: -0.1875 S13: 0.6116
REMARK 3 S21: -1.1581 S22: -0.0105 S23: -0.1977
REMARK 3 S31: -1.3607 S32: 0.1192 S33: -0.2581
REMARK 3
REMARK 3 TLS GROUP : 21
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 40 C 57
REMARK 3 ORIGIN FOR THE GROUP (A): -55.5405 -42.8028 -42.0097
REMARK 3 T TENSOR
REMARK 3 T11: 0.3745 T22: 0.3633
REMARK 3 T33: 0.2418 T12: -0.0049
REMARK 3 T13: -0.0290 T23: -0.0131
REMARK 3 L TENSOR
REMARK 3 L11: 10.7048 L22: 4.6106
REMARK 3 L33: 2.5192 L12: -0.0543
REMARK 3 L13: -1.1941 L23: 1.2957
REMARK 3 S TENSOR
REMARK 3 S11: 0.2881 S12: 0.9148 S13: -0.2322
REMARK 3 S21: -0.7482 S22: -0.2281 S23: 0.3170
REMARK 3 S31: -0.5817 S32: -0.0393 S33: -0.0600
REMARK 3
REMARK 3 TLS GROUP : 22
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : C 58 C 75
REMARK 3 ORIGIN FOR THE GROUP (A): -53.1063 -45.2677 -38.3397
REMARK 3 T TENSOR
REMARK 3 T11: 0.3137 T22: 0.3783
REMARK 3 T33: 0.2829 T12: -0.0742
REMARK 3 T13: 0.0088 T23: -0.0179
REMARK 3 L TENSOR
REMARK 3 L11: 2.3848 L22: 3.0100
REMARK 3 L33: 3.7517 L12: -1.7581
REMARK 3 L13: -2.6121 L23: 2.4261
REMARK 3 S TENSOR
REMARK 3 S11: 0.0178 S12: -0.0907 S13: 0.3397
REMARK 3 S21: -0.0862 S22: -0.0122 S23: -0.0224
REMARK 3 S31: 0.0278 S32: 0.0550 S33: -0.0056
REMARK 3
REMARK 3 TLS GROUP : 23
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 1 D 16
REMARK 3 ORIGIN FOR THE GROUP (A):-105.6727 -22.5102 -10.0500
REMARK 3 T TENSOR
REMARK 3 T11: 0.4059 T22: 0.3398
REMARK 3 T33: 0.4919 T12: -0.0891
REMARK 3 T13: 0.0522 T23: -0.1734
REMARK 3 L TENSOR
REMARK 3 L11: 9.5649 L22: 9.4715
REMARK 3 L33: 2.9559 L12: 3.9531
REMARK 3 L13: 0.0633 L23: -2.9850
REMARK 3 S TENSOR
REMARK 3 S11: -0.5828 S12: 0.1468 S13: -0.5257
REMARK 3 S21: -0.0374 S22: 0.0292 S23: 0.4872
REMARK 3 S31: 0.5536 S32: -0.4203 S33: 0.5536
REMARK 3
REMARK 3 TLS GROUP : 24
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 17 D 39
REMARK 3 ORIGIN FOR THE GROUP (A):-103.0758 -13.8639 -15.8900
REMARK 3 T TENSOR
REMARK 3 T11: 0.3814 T22: 0.3199
REMARK 3 T33: 0.2591 T12: 0.0398
REMARK 3 T13: -0.0465 T23: 0.0185
REMARK 3 L TENSOR
REMARK 3 L11: 10.5793 L22: 5.1694
REMARK 3 L33: 4.4194 L12: -5.5105
REMARK 3 L13: 0.7852 L23: 0.3391
REMARK 3 S TENSOR
REMARK 3 S11: 0.3573 S12: 1.1270 S13: 0.3187
REMARK 3 S21: -0.8135 S22: -0.1994 S23: -0.1746
REMARK 3 S31: -0.8415 S32: -0.2999 S33: -0.1579
REMARK 3
REMARK 3 TLS GROUP : 25
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 40 D 56
REMARK 3 ORIGIN FOR THE GROUP (A): -97.5378 -11.4251 -6.8727
REMARK 3 T TENSOR
REMARK 3 T11: 0.4031 T22: 0.2197
REMARK 3 T33: 0.3357 T12: -0.0344
REMARK 3 T13: 0.0118 T23: -0.0106
REMARK 3 L TENSOR
REMARK 3 L11: 11.1447 L22: 2.7789
REMARK 3 L33: 3.1511 L12: -1.1919
REMARK 3 L13: -0.6638 L23: 3.0672
REMARK 3 S TENSOR
REMARK 3 S11: 0.3602 S12: 0.0028 S13: 0.6687
REMARK 3 S21: -0.5001 S22: 0.0557 S23: -0.3849
REMARK 3 S31: -0.5641 S32: 0.1829 S33: -0.4159
REMARK 3
REMARK 3 TLS GROUP : 26
REMARK 3 NUMBER OF COMPONENTS GROUP : 1
REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI
REMARK 3 RESIDUE RANGE : D 57 D 75
REMARK 3 ORIGIN FOR THE GROUP (A): -99.1186 -15.6076 -5.3257
REMARK 3 T TENSOR
REMARK 3 T11: 0.2850 T22: 0.2138
REMARK 3 T33: 0.3441 T12: -0.0265
REMARK 3 T13: -0.0501 T23: 0.0213
REMARK 3 L TENSOR
REMARK 3 L11: 3.3145 L22: 3.9100
REMARK 3 L33: 4.9235 L12: -2.3201
REMARK 3 L13: -1.0976 L23: 3.0634
REMARK 3 S TENSOR
REMARK 3 S11: 0.0242 S12: 0.1122 S13: -0.2312
REMARK 3 S21: -0.1095 S22: 0.2341 S23: 0.1053
REMARK 3 S31: -0.2585 S32: 0.3012 S33: -0.2583
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.40
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. ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL B
REMARK 3 FACTORS. ANISOU RECORD CONTAINS SUMOF TLS AND RESIDUAL U FACTORS.
REMARK 4
REMARK 4 3IHP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-JUL-09.
REMARK 100 THE DEPOSITION ID IS D_1000054424.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 11-JUN-07
REMARK 200 TEMPERATURE (KELVIN) : 100.0
REMARK 200 PH : 6.5
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) : 0.97918
REMARK 200 MONOCHROMATOR : DOUBLE CRYSTAL
REMARK 200 OPTICS : MIRRORS
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 : 66229
REMARK 200 RESOLUTION RANGE HIGH (A) : 2.800
REMARK 200 RESOLUTION RANGE LOW (A) : 35.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : -3.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.0
REMARK 200 DATA REDUNDANCY : 5.400
REMARK 200 R MERGE (I) : NULL
REMARK 200 R SYM (I) : 0.10100
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 17.1000
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 (%) : 94.6
REMARK 200 DATA REDUNDANCY IN SHELL : 5.40
REMARK 200 R MERGE FOR SHELL (I) : NULL
REMARK 200 R SYM FOR SHELL (I) : 0.84500
REMARK 200 <I/SIGMA(I)> FOR SHELL : 2.000
REMARK 200
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT
REMARK 200 SOFTWARE USED: PHASER
REMARK 200 STARTING MODEL: PDB ENTRIES 2IBI, 2G43, 2DAK, 2DAG
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 61.82
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.22
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTALS OF THE COVALENT UBIQUITIN
REMARK 280 COMPLEX OF USP5 WERE GROWN AT 298 K USING THE HANGING DROP
REMARK 280 METHOD BY MIXING EQUAL VOLUMES OF PROTEIN SOLUTION (25 MG/ML)
REMARK 280 AND CRYSTALLIZATION BUFFER (1.45 M AMMONIUM SULFATE, 0.1 M BIS-
REMARK 280 TRIS, PH 6.5, 0.2 M SODIUM ACETATE, 5% ETHYLENEGLYCOL AND 1 MM
REMARK 280 DITHIOTHREITOL). THE CRYSTALS WERE CRYOPROTECTED BY IMMERSION IN
REMARK 280 PARATONE N IN PARAFFIN OIL 30% (V/V) AND PLACED IN LIQUID
REMARK 280 NITROGEN., VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298.0K
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 34.14750
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 103.93000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 94.42250
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 103.93000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 34.14750
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 94.42250
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
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: 4530 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 35540 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C
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: 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: 4610 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 36140 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, 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 465
REMARK 465 MISSING RESIDUES
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)
REMARK 465
REMARK 465 M RES C SSSEQI
REMARK 465 MET A -18
REMARK 465 GLY A -17
REMARK 465 SER A -16
REMARK 465 SER A -15
REMARK 465 HIS A -14
REMARK 465 HIS A -13
REMARK 465 HIS A -12
REMARK 465 HIS A -11
REMARK 465 HIS A -10
REMARK 465 HIS A -9
REMARK 465 SER A -8
REMARK 465 SER A -7
REMARK 465 GLY A -6
REMARK 465 LEU A -5
REMARK 465 VAL A -4
REMARK 465 PRO A -3
REMARK 465 ARG A -2
REMARK 465 GLY A -1
REMARK 465 SER A 0
REMARK 465 ARG A 77
REMARK 465 ARG A 78
REMARK 465 PRO A 79
REMARK 465 LYS A 80
REMARK 465 GLU A 81
REMARK 465 GLU A 82
REMARK 465 ASP A 83
REMARK 465 PRO A 84
REMARK 465 ALA A 85
REMARK 465 THR A 86
REMARK 465 GLY A 87
REMARK 465 THR A 88
REMARK 465 GLY A 89
REMARK 465 ASP A 90
REMARK 465 PRO A 91
REMARK 465 PRO A 92
REMARK 465 ARG A 93
REMARK 465 LYS A 94
REMARK 465 LYS A 95
REMARK 465 PRO A 96
REMARK 465 THR A 97
REMARK 465 ARG A 98
REMARK 465 LEU A 99
REMARK 465 ALA A 100
REMARK 465 ILE A 101
REMARK 465 GLY A 102
REMARK 465 VAL A 103
REMARK 465 GLU A 104
REMARK 465 GLY A 105
REMARK 465 GLY A 106
REMARK 465 PHE A 107
REMARK 465 ASP A 108
REMARK 465 LEU A 109
REMARK 465 SER A 110
REMARK 465 GLU A 111
REMARK 465 GLU A 112
REMARK 465 LYS A 113
REMARK 465 PHE A 114
REMARK 465 GLU A 115
REMARK 465 LEU A 116
REMARK 465 ALA A 157
REMARK 465 ASP A 158
REMARK 465 SER A 159
REMARK 465 ALA A 160
REMARK 465 SER A 161
REMARK 465 ARG A 162
REMARK 465 LYS A 163
REMARK 465 GLN A 164
REMARK 465 GLU A 165
REMARK 465 VAL A 166
REMARK 465 GLN A 167
REMARK 465 ALA A 168
REMARK 465 TRP A 169
REMARK 465 ASP A 170
REMARK 465 GLY A 171
REMARK 465 GLU A 172
REMARK 465 PHE A 224
REMARK 465 LEU A 284
REMARK 465 LYS A 285
REMARK 465 MET A 286
REMARK 465 GLN A 287
REMARK 465 LYS A 288
REMARK 465 THR A 289
REMARK 465 ASP A 290
REMARK 465 LYS A 291
REMARK 465 THR A 292
REMARK 465 MET A 293
REMARK 465 THR A 294
REMARK 465 GLU A 295
REMARK 465 LEU A 296
REMARK 465 GLU A 297
REMARK 465 ILE A 298
REMARK 465 ASP A 299
REMARK 465 MET A 300
REMARK 465 ASN A 301
REMARK 465 GLN A 302
REMARK 465 ARG A 303
REMARK 465 ILE A 304
REMARK 465 GLY A 305
REMARK 465 GLU A 306
REMARK 465 TRP A 307
REMARK 465 GLU A 308
REMARK 465 LEU A 309
REMARK 465 ILE A 310
REMARK 465 GLN A 311
REMARK 465 GLU A 312
REMARK 465 SER A 313
REMARK 465 GLY A 314
REMARK 465 VAL A 315
REMARK 465 PRO A 316
REMARK 465 LEU A 317
REMARK 465 LYS A 318
REMARK 465 TYR A 389
REMARK 465 SER A 390
REMARK 465 LYS A 391
REMARK 465 PRO A 392
REMARK 465 VAL A 393
REMARK 465 PRO A 394
REMARK 465 GLU A 395
REMARK 465 SER A 396
REMARK 465 GLY A 397
REMARK 465 ASP A 398
REMARK 465 GLY A 399
REMARK 465 GLU A 400
REMARK 465 ARG A 401
REMARK 465 VAL A 402
REMARK 465 PRO A 403
REMARK 465 GLU A 404
REMARK 465 GLN A 405
REMARK 465 LYS A 406
REMARK 465 GLU A 407
REMARK 465 VAL A 408
REMARK 465 GLN A 409
REMARK 465 ALA A 618
REMARK 465 PRO A 619
REMARK 465 PRO A 620
REMARK 465 LEU A 621
REMARK 465 VAL A 622
REMARK 465 THR A 623
REMARK 465 PRO A 624
REMARK 465 ASP A 625
REMARK 465 GLU A 626
REMARK 465 PRO A 627
REMARK 465 LYS A 628
REMARK 465 ALA A 629
REMARK 465 PRO A 630
REMARK 465 MET A 631
REMARK 465 LEU A 632
REMARK 465 ASP A 633
REMARK 465 PRO A 684A
REMARK 465 GLY A 684B
REMARK 465 SER A 684C
REMARK 465 SER A 684D
REMARK 465 GLY A 684E
REMARK 465 PRO A 684F
REMARK 465 GLY A 684G
REMARK 465 SER A 684H
REMARK 465 THR A 684I
REMARK 465 SER A 684J
REMARK 465 ALA A 684K
REMARK 465 ALA A 684L
REMARK 465 ALA A 684M
REMARK 465 ASP A 684N
REMARK 465 ILE A 751
REMARK 465 SER A 752
REMARK 465 GLU A 753
REMARK 465 GLY A 754
REMARK 465 ARG A 755
REMARK 465 SER A 756
REMARK 465 ALA A 757
REMARK 465 ALA A 758
REMARK 465 ASP A 759
REMARK 465 SER A 760
REMARK 465 ILE A 761
REMARK 465 SER A 762
REMARK 465 GLU A 763
REMARK 465 SER A 764
REMARK 465 VAL A 765
REMARK 465 PRO A 766
REMARK 465 VAL A 767
REMARK 465 GLY A 768
REMARK 465 SER A 835
REMARK 465 MET B -18
REMARK 465 GLY B -17
REMARK 465 SER B -16
REMARK 465 SER B -15
REMARK 465 HIS B -14
REMARK 465 HIS B -13
REMARK 465 HIS B -12
REMARK 465 HIS B -11
REMARK 465 HIS B -10
REMARK 465 HIS B -9
REMARK 465 SER B -8
REMARK 465 SER B -7
REMARK 465 GLY B -6
REMARK 465 LEU B -5
REMARK 465 VAL B -4
REMARK 465 PRO B -3
REMARK 465 ARG B -2
REMARK 465 GLY B -1
REMARK 465 SER B 0
REMARK 465 ARG B 77
REMARK 465 ARG B 78
REMARK 465 PRO B 79
REMARK 465 LYS B 80
REMARK 465 GLU B 81
REMARK 465 GLU B 82
REMARK 465 ASP B 83
REMARK 465 PRO B 84
REMARK 465 ALA B 85
REMARK 465 THR B 86
REMARK 465 GLY B 87
REMARK 465 THR B 88
REMARK 465 GLY B 89
REMARK 465 ASP B 90
REMARK 465 PRO B 91
REMARK 465 PRO B 92
REMARK 465 ARG B 93
REMARK 465 LYS B 94
REMARK 465 LYS B 95
REMARK 465 PRO B 96
REMARK 465 THR B 97
REMARK 465 ARG B 98
REMARK 465 LEU B 99
REMARK 465 ALA B 100
REMARK 465 ILE B 101
REMARK 465 GLY B 102
REMARK 465 VAL B 103
REMARK 465 GLU B 104
REMARK 465 GLY B 105
REMARK 465 GLY B 106
REMARK 465 PHE B 107
REMARK 465 ASP B 108
REMARK 465 LEU B 109
REMARK 465 SER B 110
REMARK 465 GLU B 111
REMARK 465 GLU B 112
REMARK 465 LYS B 113
REMARK 465 PHE B 114
REMARK 465 GLU B 115
REMARK 465 LEU B 116
REMARK 465 ALA B 157
REMARK 465 ASP B 158
REMARK 465 SER B 159
REMARK 465 ALA B 160
REMARK 465 SER B 161
REMARK 465 ARG B 162
REMARK 465 LYS B 163
REMARK 465 GLN B 164
REMARK 465 GLU B 165
REMARK 465 VAL B 166
REMARK 465 GLN B 167
REMARK 465 ALA B 168
REMARK 465 TRP B 169
REMARK 465 ASP B 170
REMARK 465 GLY B 171
REMARK 465 GLU B 172
REMARK 465 LEU B 284
REMARK 465 LYS B 285
REMARK 465 MET B 286
REMARK 465 GLN B 287
REMARK 465 LYS B 288
REMARK 465 THR B 289
REMARK 465 ASP B 290
REMARK 465 LYS B 291
REMARK 465 THR B 292
REMARK 465 MET B 293
REMARK 465 THR B 294
REMARK 465 GLU B 295
REMARK 465 LEU B 296
REMARK 465 GLU B 297
REMARK 465 ILE B 298
REMARK 465 ASP B 299
REMARK 465 MET B 300
REMARK 465 ASN B 301
REMARK 465 GLN B 302
REMARK 465 ARG B 303
REMARK 465 ILE B 304
REMARK 465 GLY B 305
REMARK 465 GLU B 306
REMARK 465 TRP B 307
REMARK 465 GLU B 308
REMARK 465 LEU B 309
REMARK 465 ILE B 310
REMARK 465 GLN B 311
REMARK 465 GLU B 312
REMARK 465 SER B 313
REMARK 465 GLY B 314
REMARK 465 VAL B 315
REMARK 465 TYR B 389
REMARK 465 SER B 390
REMARK 465 LYS B 391
REMARK 465 PRO B 392
REMARK 465 VAL B 393
REMARK 465 PRO B 394
REMARK 465 GLU B 395
REMARK 465 SER B 396
REMARK 465 GLY B 397
REMARK 465 ASP B 398
REMARK 465 GLY B 399
REMARK 465 GLU B 400
REMARK 465 ARG B 401
REMARK 465 VAL B 402
REMARK 465 PRO B 403
REMARK 465 GLU B 404
REMARK 465 GLN B 405
REMARK 465 LYS B 406
REMARK 465 GLU B 407
REMARK 465 VAL B 408
REMARK 465 GLN B 409
REMARK 465 ASP B 410
REMARK 465 ALA B 618
REMARK 465 PRO B 619
REMARK 465 PRO B 620
REMARK 465 LEU B 621
REMARK 465 VAL B 622
REMARK 465 THR B 623
REMARK 465 PRO B 624
REMARK 465 ASP B 625
REMARK 465 GLU B 626
REMARK 465 PRO B 627
REMARK 465 LYS B 628
REMARK 465 ALA B 629
REMARK 465 PRO B 630
REMARK 465 MET B 631
REMARK 465 PRO B 685
REMARK 465 GLY B 686
REMARK 465 SER B 687
REMARK 465 SER B 688
REMARK 465 GLY B 689
REMARK 465 PRO B 690
REMARK 465 GLY B 691
REMARK 465 SER B 692
REMARK 465 THR B 693
REMARK 465 SER B 694
REMARK 465 ALA B 695
REMARK 465 ALA B 696
REMARK 465 ALA B 697
REMARK 465 ILE B 751
REMARK 465 SER B 752
REMARK 465 GLU B 753
REMARK 465 GLY B 754
REMARK 465 ARG B 755
REMARK 465 SER B 756
REMARK 465 ALA B 757
REMARK 465 ALA B 758
REMARK 465 ASP B 759
REMARK 465 SER B 760
REMARK 465 ILE B 761
REMARK 465 SER B 762
REMARK 465 GLU B 763
REMARK 465 SER B 764
REMARK 465 VAL B 765
REMARK 465 PRO B 766
REMARK 465 VAL B 767
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 ARG A 17 NE CZ NH1 NH2
REMARK 470 ARG A 24 CG CD NE CZ NH1 NH2
REMARK 470 ASP A 28 CG OD1 OD2
REMARK 470 LYS A 55 CG CD CE NZ
REMARK 470 GLN A 175 CG CD OE1 NE2
REMARK 470 LYS A 178 CG CD CE NZ
REMARK 470 SER A 182 OG
REMARK 470 LYS A 184 CG CD CE NZ
REMARK 470 ARG A 191 CD NE CZ NH1 NH2
REMARK 470 LYS A 198 CG CD CE NZ
REMARK 470 GLU A 206 CG CD OE1 OE2
REMARK 470 ARG A 222 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 360 CE NZ
REMARK 470 ASN A 364 CG OD1 ND2
REMARK 470 LYS A 423 CE NZ
REMARK 470 GLU A 500 CG CD OE1 OE2
REMARK 470 GLU A 504 CG CD OE1 OE2
REMARK 470 LYS A 508 CG CD CE NZ
REMARK 470 LYS A 509 CG CD CE NZ
REMARK 470 LYS A 516 CG CD CE NZ
REMARK 470 LYS A 553 NZ
REMARK 470 GLN A 601 CG CD OE1 NE2
REMARK 470 ASP A 648 CG OD1 OD2
REMARK 470 LYS A 770 CG CD CE NZ
REMARK 470 LYS A 813 CD CE NZ
REMARK 470 LYS A 822 CE NZ
REMARK 470 ARG B 17 NE CZ NH1 NH2
REMARK 470 ARG B 24 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 28 CG OD1 OD2
REMARK 470 LYS B 55 CG CD CE NZ
REMARK 470 LYS B 121 CE NZ
REMARK 470 GLN B 175 CG CD OE1 NE2
REMARK 470 LYS B 178 CG CD CE NZ
REMARK 470 LYS B 184 CG CD CE NZ
REMARK 470 ARG B 191 CD NE CZ NH1 NH2
REMARK 470 LYS B 198 CG CD CE NZ
REMARK 470 LYS B 201 CG CD CE NZ
REMARK 470 ASP B 203 CG OD1 OD2
REMARK 470 ARG B 205 CG CD NE CZ NH1 NH2
REMARK 470 ASP B 282 CG OD1 OD2
REMARK 470 LYS B 379 NZ
REMARK 470 GLU B 500 CG CD OE1 OE2
REMARK 470 LYS B 509 CG CD CE NZ
REMARK 470 GLU B 513 CG CD OE1 OE2
REMARK 470 LYS B 516 CG CD CE NZ
REMARK 470 LEU B 580 CG CD1 CD2
REMARK 470 LYS B 585 NZ
REMARK 470 ASP B 633 CG OD1 OD2
REMARK 470 ASP B 698 CG OD1 OD2
REMARK 470 MET B 749 CG SD CE
REMARK 470 LYS B 770 CG CD CE NZ
REMARK 470 LYS B 819 CG CD CE NZ
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 O GLY D 75 N NEH D 76 2.18
REMARK 500
REMARK 500 REMARK: NULL
REMARK 500
REMARK 500 GEOMETRY AND STEREOCHEMISTRY
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS
REMARK 500
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).
REMARK 500
REMARK 500 STANDARD TABLE:
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)
REMARK 500
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996
REMARK 500
REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION
REMARK 500 ARG B 715 NE ARG B 715 CZ 0.087
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 LEU A 155 32.71 -78.98
REMARK 500 CYS A 202 -136.49 -96.01
REMARK 500 MET A 204 135.97 -33.49
REMARK 500 ASP A 264 61.25 37.15
REMARK 500 SER A 386 -131.93 -109.59
REMARK 500 SER A 453 53.79 36.44
REMARK 500 ASP A 494 -9.59 -59.80
REMARK 500 ALA A 496 129.99 -37.80
REMARK 500 ASN A 498 43.56 -140.52
REMARK 500 SER A 554 -149.14 -142.59
REMARK 500 SER A 564 137.91 178.47
REMARK 500 ASP A 616 -156.30 -125.72
REMARK 500 ASP A 811 -111.17 42.86
REMARK 500 ASP A 811 -110.93 42.86
REMARK 500 LYS A 819 64.09 -116.31
REMARK 500 LYS A 822 5.35 -65.77
REMARK 500 CYS B 195 179.60 179.97
REMARK 500 LYS B 201 -72.02 -89.91
REMARK 500 CYS B 202 -158.09 -77.26
REMARK 500 MET B 204 150.31 -49.13
REMARK 500 ASN B 207 45.09 70.76
REMARK 500 PHE B 224 37.55 -77.42
REMARK 500 SER B 386 -133.75 -103.19
REMARK 500 PRO B 414 42.75 -84.89
REMARK 500 ASP B 494 22.06 -75.37
REMARK 500 GLU B 521 125.01 -37.53
REMARK 500 SER B 554 -156.42 -148.45
REMARK 500 ASP B 616 -168.21 -101.90
REMARK 500 ASP B 633 -147.00 -137.32
REMARK 500 ASN B 727 5.80 58.86
REMARK 500 SER B 728 97.97 -67.03
REMARK 500 ASP B 811 -118.83 46.77
REMARK 500 GLU B 818 -72.73 -98.52
REMARK 500 ALA B 834 2.85 -67.85
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 836 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS A 199 SG
REMARK 620 2 CYS A 202 SG 111.5
REMARK 620 3 CYS A 219 SG 129.1 110.2
REMARK 620 4 HIS A 232 ND1 94.6 103.2 103.1
REMARK 620 N 1 2 3
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 ZN B 836 ZN
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 CYS B 199 SG
REMARK 620 2 CYS B 202 SG 104.1
REMARK 620 3 CYS B 219 SG 122.2 84.6
REMARK 620 4 HIS B 232 ND1 127.1 113.0 98.2
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 NEH C 76
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NEH D 76
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 77
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN A 836
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN B 836
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 2DAG RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE FIRST UBA DOMAIN IN THE HUMAN UBIQUITIN
REMARK 900 SPECIFIC PROTEASE 5 (ISOPEPTIDASE 5)
REMARK 900 RELATED ID: 2DAK RELATED DB: PDB
REMARK 900 SOLUTION STRUCTURE OF THE SECOND UBA DOMAIN IN THE HUMAN UBIQUITIN
REMARK 900 SPECIFIC PROTEASE 5 (ISOPEPTIDASE 5)
REMARK 900 RELATED ID: 2G43 RELATED DB: PDB
REMARK 900 STRUCTURE OF THE ZNF UBP DOMAIN FROM DEUBIQUITINATING ENZYME
REMARK 900 ISOPEPTIDASE T (ISOT)
DBREF 3IHP A 1 835 UNP P45974-2 UBP5_HUMAN 1 835
DBREF 3IHP B 1 835 UNP P45974-2 UBP5_HUMAN 1 835
DBREF 3IHP C 1 75 UNP P62988 UBIQ_HUMAN 1 75
DBREF 3IHP D 1 75 UNP P62988 UBIQ_HUMAN 1 75
SEQADV 3IHP MET A -18 UNP P45974-2 EXPRESSION TAG
SEQADV 3IHP GLY A -17 UNP P45974-2 EXPRESSION TAG
SEQADV 3IHP SER A -16 UNP P45974-2 EXPRESSION TAG
SEQADV 3IHP SER A -15 UNP P45974-2 EXPRESSION TAG
SEQADV 3IHP HIS A -14 UNP P45974-2 EXPRESSION TAG
SEQADV 3IHP HIS A -13 UNP P45974-2 EXPRESSION TAG
SEQADV 3IHP HIS A -12 UNP P45974-2 EXPRESSION TAG
SEQADV 3IHP HIS A -11 UNP P45974-2 EXPRESSION TAG
SEQADV 3IHP HIS A -10 UNP P45974-2 EXPRESSION TAG
SEQADV 3IHP HIS A -9 UNP P45974-2 EXPRESSION TAG
SEQADV 3IHP SER A -8 UNP P45974-2 EXPRESSION TAG
SEQADV 3IHP SER A -7 UNP P45974-2 EXPRESSION TAG
SEQADV 3IHP GLY A -6 UNP P45974-2 EXPRESSION TAG
SEQADV 3IHP LEU A -5 UNP P45974-2 EXPRESSION TAG
SEQADV 3IHP VAL A -4 UNP P45974-2 EXPRESSION TAG
SEQADV 3IHP PRO A -3 UNP P45974-2 EXPRESSION TAG
SEQADV 3IHP ARG A -2 UNP P45974-2 EXPRESSION TAG
SEQADV 3IHP GLY A -1 UNP P45974-2 EXPRESSION TAG
SEQADV 3IHP SER A 0 UNP P45974-2 EXPRESSION TAG
SEQADV 3IHP MET B -18 UNP P45974-2 EXPRESSION TAG
SEQADV 3IHP GLY B -17 UNP P45974-2 EXPRESSION TAG
SEQADV 3IHP SER B -16 UNP P45974-2 EXPRESSION TAG
SEQADV 3IHP SER B -15 UNP P45974-2 EXPRESSION TAG
SEQADV 3IHP HIS B -14 UNP P45974-2 EXPRESSION TAG
SEQADV 3IHP HIS B -13 UNP P45974-2 EXPRESSION TAG
SEQADV 3IHP HIS B -12 UNP P45974-2 EXPRESSION TAG
SEQADV 3IHP HIS B -11 UNP P45974-2 EXPRESSION TAG
SEQADV 3IHP HIS B -10 UNP P45974-2 EXPRESSION TAG
SEQADV 3IHP HIS B -9 UNP P45974-2 EXPRESSION TAG
SEQADV 3IHP SER B -8 UNP P45974-2 EXPRESSION TAG
SEQADV 3IHP SER B -7 UNP P45974-2 EXPRESSION TAG
SEQADV 3IHP GLY B -6 UNP P45974-2 EXPRESSION TAG
SEQADV 3IHP LEU B -5 UNP P45974-2 EXPRESSION TAG
SEQADV 3IHP VAL B -4 UNP P45974-2 EXPRESSION TAG
SEQADV 3IHP PRO B -3 UNP P45974-2 EXPRESSION TAG
SEQADV 3IHP ARG B -2 UNP P45974-2 EXPRESSION TAG
SEQADV 3IHP GLY B -1 UNP P45974-2 EXPRESSION TAG
SEQADV 3IHP SER B 0 UNP P45974-2 EXPRESSION TAG
SEQRES 1 A 854 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 A 854 LEU VAL PRO ARG GLY SER MET ALA GLU LEU SER GLU GLU
SEQRES 3 A 854 ALA LEU LEU SER VAL LEU PRO THR ILE ARG VAL PRO LYS
SEQRES 4 A 854 ALA GLY ASP ARG VAL HIS LYS ASP GLU CYS ALA PHE SER
SEQRES 5 A 854 PHE ASP THR PRO GLU SER GLU GLY GLY LEU TYR ILE CYS
SEQRES 6 A 854 MET ASN THR PHE LEU GLY PHE GLY LYS GLN TYR VAL GLU
SEQRES 7 A 854 ARG HIS PHE ASN LYS THR GLY GLN ARG VAL TYR LEU HIS
SEQRES 8 A 854 LEU ARG ARG THR ARG ARG PRO LYS GLU GLU ASP PRO ALA
SEQRES 9 A 854 THR GLY THR GLY ASP PRO PRO ARG LYS LYS PRO THR ARG
SEQRES 10 A 854 LEU ALA ILE GLY VAL GLU GLY GLY PHE ASP LEU SER GLU
SEQRES 11 A 854 GLU LYS PHE GLU LEU ASP GLU ASP VAL LYS ILE VAL ILE
SEQRES 12 A 854 LEU PRO ASP TYR LEU GLU ILE ALA ARG ASP GLY LEU GLY
SEQRES 13 A 854 GLY LEU PRO ASP ILE VAL ARG ASP ARG VAL THR SER ALA
SEQRES 14 A 854 VAL GLU ALA LEU LEU SER ALA ASP SER ALA SER ARG LYS
SEQRES 15 A 854 GLN GLU VAL GLN ALA TRP ASP GLY GLU VAL ARG GLN VAL
SEQRES 16 A 854 SER LYS HIS ALA PHE SER LEU LYS GLN LEU ASP ASN PRO
SEQRES 17 A 854 ALA ARG ILE PRO PRO CYS GLY TRP LYS CYS SER LYS CYS
SEQRES 18 A 854 ASP MET ARG GLU ASN LEU TRP LEU ASN LEU THR ASP GLY
SEQRES 19 A 854 SER ILE LEU CYS GLY ARG ARG TYR PHE ASP GLY SER GLY
SEQRES 20 A 854 GLY ASN ASN HIS ALA VAL GLU HIS TYR ARG GLU THR GLY
SEQRES 21 A 854 TYR PRO LEU ALA VAL LYS LEU GLY THR ILE THR PRO ASP
SEQRES 22 A 854 GLY ALA ASP VAL TYR SER TYR ASP GLU ASP ASP MET VAL
SEQRES 23 A 854 LEU ASP PRO SER LEU ALA GLU HIS LEU SER HIS PHE GLY
SEQRES 24 A 854 ILE ASP MET LEU LYS MET GLN LYS THR ASP LYS THR MET
SEQRES 25 A 854 THR GLU LEU GLU ILE ASP MET ASN GLN ARG ILE GLY GLU
SEQRES 26 A 854 TRP GLU LEU ILE GLN GLU SER GLY VAL PRO LEU LYS PRO
SEQRES 27 A 854 LEU PHE GLY PRO GLY TYR THR GLY ILE ARG ASN LEU GLY
SEQRES 28 A 854 ASN SER CYS TYR LEU ASN SER VAL VAL GLN VAL LEU PHE
SEQRES 29 A 854 SER ILE PRO ASP PHE GLN ARG LYS TYR VAL ASP LYS LEU
SEQRES 30 A 854 GLU LYS ILE PHE GLN ASN ALA PRO THR ASP PRO THR GLN
SEQRES 31 A 854 ASP PHE SER THR GLN VAL ALA LYS LEU GLY HIS GLY LEU
SEQRES 32 A 854 LEU SER GLY GLU TYR SER LYS PRO VAL PRO GLU SER GLY
SEQRES 33 A 854 ASP GLY GLU ARG VAL PRO GLU GLN LYS GLU VAL GLN ASP
SEQRES 34 A 854 GLY ILE ALA PRO ARG MET PHE LYS ALA LEU ILE GLY LYS
SEQRES 35 A 854 GLY HIS PRO GLU PHE SER THR ASN ARG GLN GLN ASP ALA
SEQRES 36 A 854 GLN GLU PHE PHE LEU HIS LEU ILE ASN MET VAL GLU ARG
SEQRES 37 A 854 ASN CYS ARG SER SER GLU ASN PRO ASN GLU VAL PHE ARG
SEQRES 38 A 854 PHE LEU VAL GLU GLU LYS ILE LYS CYS LEU ALA THR GLU
SEQRES 39 A 854 LYS VAL LYS TYR THR GLN ARG VAL ASP TYR ILE MET GLN
SEQRES 40 A 854 LEU PRO VAL PRO MET ASP ALA ALA LEU ASN LYS GLU GLU
SEQRES 41 A 854 LEU LEU GLU TYR GLU GLU LYS LYS ARG GLN ALA GLU GLU
SEQRES 42 A 854 GLU LYS MET ALA LEU PRO GLU LEU VAL ARG ALA GLN VAL
SEQRES 43 A 854 PRO PHE SER SER CYS LEU GLU ALA TYR GLY ALA PRO GLU
SEQRES 44 A 854 GLN VAL ASP ASP PHE TRP SER THR ALA LEU GLN ALA LYS
SEQRES 45 A 854 SER VAL ALA VAL LYS THR THR ARG PHE ALA SER PHE PRO
SEQRES 46 A 854 ASP TYR LEU VAL ILE GLN ILE LYS LYS PHE THR PHE GLY
SEQRES 47 A 854 LEU ASP TRP VAL PRO LYS LYS LEU ASP VAL SER ILE GLU
SEQRES 48 A 854 MET PRO GLU GLU LEU ASP ILE SER GLN LEU ARG GLY THR
SEQRES 49 A 854 GLY LEU GLN PRO GLY GLU GLU GLU LEU PRO ASP ILE ALA
SEQRES 50 A 854 PRO PRO LEU VAL THR PRO ASP GLU PRO LYS ALA PRO MET
SEQRES 51 A 854 LEU ASP GLU SER VAL ILE ILE GLN LEU VAL GLU MET GLY
SEQRES 52 A 854 PHE PRO MET ASP ALA CYS ARG LYS ALA VAL TYR TYR THR
SEQRES 53 A 854 GLY ASN SER GLY ALA GLU ALA ALA MET ASN TRP VAL MET
SEQRES 54 A 854 SER HIS MET ASP ASP PRO ASP PHE ALA ASN PRO LEU ILE
SEQRES 55 A 854 LEU PRO GLY SER SER GLY PRO GLY SER THR SER ALA ALA
SEQRES 56 A 854 ALA ASP PRO PRO PRO GLU ASP CYS VAL THR THR ILE VAL
SEQRES 57 A 854 SER MET GLY PHE SER ARG ASP GLN ALA LEU LYS ALA LEU
SEQRES 58 A 854 ARG ALA THR ASN ASN SER LEU GLU ARG ALA VAL ASP TRP
SEQRES 59 A 854 ILE PHE SER HIS ILE ASP ASP LEU ASP ALA GLU ALA ALA
SEQRES 60 A 854 MET ASP ILE SER GLU GLY ARG SER ALA ALA ASP SER ILE
SEQRES 61 A 854 SER GLU SER VAL PRO VAL GLY PRO LYS VAL ARG ASP GLY
SEQRES 62 A 854 PRO GLY LYS TYR GLN LEU PHE ALA PHE ILE SER HIS MET
SEQRES 63 A 854 GLY THR SER THR MET CYS GLY HIS TYR VAL CYS HIS ILE
SEQRES 64 A 854 LYS LYS GLU GLY ARG TRP VAL ILE TYR ASN ASP GLN LYS
SEQRES 65 A 854 VAL CYS ALA SER GLU LYS PRO PRO LYS ASP LEU GLY TYR
SEQRES 66 A 854 ILE TYR PHE TYR GLN ARG VAL ALA SER
SEQRES 1 B 854 MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY
SEQRES 2 B 854 LEU VAL PRO ARG GLY SER MET ALA GLU LEU SER GLU GLU
SEQRES 3 B 854 ALA LEU LEU SER VAL LEU PRO THR ILE ARG VAL PRO LYS
SEQRES 4 B 854 ALA GLY ASP ARG VAL HIS LYS ASP GLU CYS ALA PHE SER
SEQRES 5 B 854 PHE ASP THR PRO GLU SER GLU GLY GLY LEU TYR ILE CYS
SEQRES 6 B 854 MET ASN THR PHE LEU GLY PHE GLY LYS GLN TYR VAL GLU
SEQRES 7 B 854 ARG HIS PHE ASN LYS THR GLY GLN ARG VAL TYR LEU HIS
SEQRES 8 B 854 LEU ARG ARG THR ARG ARG PRO LYS GLU GLU ASP PRO ALA
SEQRES 9 B 854 THR GLY THR GLY ASP PRO PRO ARG LYS LYS PRO THR ARG
SEQRES 10 B 854 LEU ALA ILE GLY VAL GLU GLY GLY PHE ASP LEU SER GLU
SEQRES 11 B 854 GLU LYS PHE GLU LEU ASP GLU ASP VAL LYS ILE VAL ILE
SEQRES 12 B 854 LEU PRO ASP TYR LEU GLU ILE ALA ARG ASP GLY LEU GLY
SEQRES 13 B 854 GLY LEU PRO ASP ILE VAL ARG ASP ARG VAL THR SER ALA
SEQRES 14 B 854 VAL GLU ALA LEU LEU SER ALA ASP SER ALA SER ARG LYS
SEQRES 15 B 854 GLN GLU VAL GLN ALA TRP ASP GLY GLU VAL ARG GLN VAL
SEQRES 16 B 854 SER LYS HIS ALA PHE SER LEU LYS GLN LEU ASP ASN PRO
SEQRES 17 B 854 ALA ARG ILE PRO PRO CYS GLY TRP LYS CYS SER LYS CYS
SEQRES 18 B 854 ASP MET ARG GLU ASN LEU TRP LEU ASN LEU THR ASP GLY
SEQRES 19 B 854 SER ILE LEU CYS GLY ARG ARG TYR PHE ASP GLY SER GLY
SEQRES 20 B 854 GLY ASN ASN HIS ALA VAL GLU HIS TYR ARG GLU THR GLY
SEQRES 21 B 854 TYR PRO LEU ALA VAL LYS LEU GLY THR ILE THR PRO ASP
SEQRES 22 B 854 GLY ALA ASP VAL TYR SER TYR ASP GLU ASP ASP MET VAL
SEQRES 23 B 854 LEU ASP PRO SER LEU ALA GLU HIS LEU SER HIS PHE GLY
SEQRES 24 B 854 ILE ASP MET LEU LYS MET GLN LYS THR ASP LYS THR MET
SEQRES 25 B 854 THR GLU LEU GLU ILE ASP MET ASN GLN ARG ILE GLY GLU
SEQRES 26 B 854 TRP GLU LEU ILE GLN GLU SER GLY VAL PRO LEU LYS PRO
SEQRES 27 B 854 LEU PHE GLY PRO GLY TYR THR GLY ILE ARG ASN LEU GLY
SEQRES 28 B 854 ASN SER CYS TYR LEU ASN SER VAL VAL GLN VAL LEU PHE
SEQRES 29 B 854 SER ILE PRO ASP PHE GLN ARG LYS TYR VAL ASP LYS LEU
SEQRES 30 B 854 GLU LYS ILE PHE GLN ASN ALA PRO THR ASP PRO THR GLN
SEQRES 31 B 854 ASP PHE SER THR GLN VAL ALA LYS LEU GLY HIS GLY LEU
SEQRES 32 B 854 LEU SER GLY GLU TYR SER LYS PRO VAL PRO GLU SER GLY
SEQRES 33 B 854 ASP GLY GLU ARG VAL PRO GLU GLN LYS GLU VAL GLN ASP
SEQRES 34 B 854 GLY ILE ALA PRO ARG MET PHE LYS ALA LEU ILE GLY LYS
SEQRES 35 B 854 GLY HIS PRO GLU PHE SER THR ASN ARG GLN GLN ASP ALA
SEQRES 36 B 854 GLN GLU PHE PHE LEU HIS LEU ILE ASN MET VAL GLU ARG
SEQRES 37 B 854 ASN CYS ARG SER SER GLU ASN PRO ASN GLU VAL PHE ARG
SEQRES 38 B 854 PHE LEU VAL GLU GLU LYS ILE LYS CYS LEU ALA THR GLU
SEQRES 39 B 854 LYS VAL LYS TYR THR GLN ARG VAL ASP TYR ILE MET GLN
SEQRES 40 B 854 LEU PRO VAL PRO MET ASP ALA ALA LEU ASN LYS GLU GLU
SEQRES 41 B 854 LEU LEU GLU TYR GLU GLU LYS LYS ARG GLN ALA GLU GLU
SEQRES 42 B 854 GLU LYS MET ALA LEU PRO GLU LEU VAL ARG ALA GLN VAL
SEQRES 43 B 854 PRO PHE SER SER CYS LEU GLU ALA TYR GLY ALA PRO GLU
SEQRES 44 B 854 GLN VAL ASP ASP PHE TRP SER THR ALA LEU GLN ALA LYS
SEQRES 45 B 854 SER VAL ALA VAL LYS THR THR ARG PHE ALA SER PHE PRO
SEQRES 46 B 854 ASP TYR LEU VAL ILE GLN ILE LYS LYS PHE THR PHE GLY
SEQRES 47 B 854 LEU ASP TRP VAL PRO LYS LYS LEU ASP VAL SER ILE GLU
SEQRES 48 B 854 MET PRO GLU GLU LEU ASP ILE SER GLN LEU ARG GLY THR
SEQRES 49 B 854 GLY LEU GLN PRO GLY GLU GLU GLU LEU PRO ASP ILE ALA
SEQRES 50 B 854 PRO PRO LEU VAL THR PRO ASP GLU PRO LYS ALA PRO MET
SEQRES 51 B 854 LEU ASP GLU SER VAL ILE ILE GLN LEU VAL GLU MET GLY
SEQRES 52 B 854 PHE PRO MET ASP ALA CYS ARG LYS ALA VAL TYR TYR THR
SEQRES 53 B 854 GLY ASN SER GLY ALA GLU ALA ALA MET ASN TRP VAL MET
SEQRES 54 B 854 SER HIS MET ASP ASP PRO ASP PHE ALA ASN PRO LEU ILE
SEQRES 55 B 854 LEU PRO GLY SER SER GLY PRO GLY SER THR SER ALA ALA
SEQRES 56 B 854 ALA ASP PRO PRO PRO GLU ASP CYS VAL THR THR ILE VAL
SEQRES 57 B 854 SER MET GLY PHE SER ARG ASP GLN ALA LEU LYS ALA LEU
SEQRES 58 B 854 ARG ALA THR ASN ASN SER LEU GLU ARG ALA VAL ASP TRP
SEQRES 59 B 854 ILE PHE SER HIS ILE ASP ASP LEU ASP ALA GLU ALA ALA
SEQRES 60 B 854 MET ASP ILE SER GLU GLY ARG SER ALA ALA ASP SER ILE
SEQRES 61 B 854 SER GLU SER VAL PRO VAL GLY PRO LYS VAL ARG ASP GLY
SEQRES 62 B 854 PRO GLY LYS TYR GLN LEU PHE ALA PHE ILE SER HIS MET
SEQRES 63 B 854 GLY THR SER THR MET CYS GLY HIS TYR VAL CYS HIS ILE
SEQRES 64 B 854 LYS LYS GLU GLY ARG TRP VAL ILE TYR ASN ASP GLN LYS
SEQRES 65 B 854 VAL CYS ALA SER GLU LYS PRO PRO LYS ASP LEU GLY TYR
SEQRES 66 B 854 ILE TYR PHE TYR GLN ARG VAL ALA SER
SEQRES 1 C 75 MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE
SEQRES 2 C 75 THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL
SEQRES 3 C 75 LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP
SEQRES 4 C 75 GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP
SEQRES 5 C 75 GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER
SEQRES 6 C 75 THR LEU HIS LEU VAL LEU ARG LEU ARG GLY
SEQRES 1 D 75 MET GLN ILE PHE VAL LYS THR LEU THR GLY LYS THR ILE
SEQRES 2 D 75 THR LEU GLU VAL GLU PRO SER ASP THR ILE GLU ASN VAL
SEQRES 3 D 75 LYS ALA LYS ILE GLN ASP LYS GLU GLY ILE PRO PRO ASP
SEQRES 4 D 75 GLN GLN ARG LEU ILE PHE ALA GLY LYS GLN LEU GLU ASP
SEQRES 5 D 75 GLY ARG THR LEU SER ASP TYR ASN ILE GLN LYS GLU SER
SEQRES 6 D 75 THR LEU HIS LEU VAL LEU ARG LEU ARG GLY
HET ZN A 836 1
HET ZN B 836 1
HET NEH C 76 3
HET NEH D 76 3
HET CL D 77 1
HETNAM ZN ZINC ION
HETNAM NEH ETHANAMINE
HETNAM CL CHLORIDE ION
FORMUL 5 ZN 2(ZN 2+)
FORMUL 7 NEH 2(C2 H7 N)
FORMUL 9 CL CL 1-
FORMUL 10 HOH *32(H2 O)
HELIX 1 1 LEU A 4 VAL A 12 1 9
HELIX 2 2 LEU A 13 ILE A 16 5 4
HELIX 3 3 TYR A 57 GLY A 66 1 10
HELIX 4 4 PRO A 140 LEU A 155 1 16
HELIX 5 5 ASN A 231 GLY A 241 1 11
HELIX 6 6 SER A 271 PHE A 279 1 9
HELIX 7 7 SER A 334 PHE A 345 1 12
HELIX 8 8 ILE A 347 VAL A 355 1 9
HELIX 9 9 LYS A 357 ALA A 365 1 9
HELIX 10 10 ASP A 368 GLN A 371 5 4
HELIX 11 11 ASP A 372 SER A 386 1 15
HELIX 12 12 PRO A 414 GLY A 422 1 9
HELIX 13 13 ALA A 436 ASN A 450 1 15
HELIX 14 14 ASN A 456 PHE A 461 5 6
HELIX 15 15 PRO A 492 ALA A 496 5 5
HELIX 16 16 ASN A 498 GLU A 515 1 18
HELIX 17 17 PRO A 528 ALA A 538 1 11
HELIX 18 18 LEU A 580 TRP A 582 5 3
HELIX 19 19 SER A 600 ARG A 603 5 4
HELIX 20 20 GLU A 634 GLY A 644 1 11
HELIX 21 21 PRO A 646 THR A 657 1 12
HELIX 22 22 GLY A 661 MET A 673 1 13
HELIX 23 23 PRO A 676 ASN A 680 5 5
HELIX 24 24 PRO A 700 SER A 709 1 10
HELIX 25 25 SER A 713 THR A 724 1 12
HELIX 26 26 SER A 727 ALA A 747 1 21
HELIX 27 27 LEU B 4 SER B 11 1 8
HELIX 28 28 VAL B 12 ILE B 16 5 5
HELIX 29 29 TYR B 57 GLY B 66 1 10
HELIX 30 30 PRO B 140 LEU B 155 1 16
HELIX 31 31 ASN B 231 GLY B 241 1 11
HELIX 32 32 SER B 271 HIS B 278 1 8
HELIX 33 33 SER B 334 PHE B 345 1 12
HELIX 34 34 ILE B 347 VAL B 355 1 9
HELIX 35 35 LYS B 357 ASN B 364 1 8
HELIX 36 36 ASP B 368 GLN B 371 5 4
HELIX 37 37 ASP B 372 SER B 386 1 15
HELIX 38 38 PRO B 414 LYS B 423 1 10
HELIX 39 39 ASP B 435 CYS B 451 1 17
HELIX 40 40 ASN B 456 PHE B 461 5 6
HELIX 41 41 PRO B 492 ALA B 496 5 5
HELIX 42 42 ASN B 498 LYS B 516 1 19
HELIX 43 43 PRO B 528 ALA B 538 1 11
HELIX 44 44 LEU B 580 TRP B 582 5 3
HELIX 45 45 SER B 600 ARG B 603 5 4
HELIX 46 46 GLU B 634 GLU B 642 1 9
HELIX 47 47 PRO B 646 TYR B 656 1 11
HELIX 48 48 GLY B 661 MET B 673 1 13
HELIX 49 49 PRO B 701 SER B 710 1 10
HELIX 50 50 SER B 714 THR B 725 1 12
HELIX 51 51 SER B 728 MET B 749 1 22
HELIX 52 52 THR C 22 GLY C 35 1 14
HELIX 53 53 PRO C 37 GLN C 41 5 5
HELIX 54 54 THR D 22 GLY D 35 1 14
HELIX 55 55 PRO D 37 GLN D 41 5 5
SHEET 1 A 5 GLY A 52 PHE A 53 0
SHEET 2 A 5 LEU A 43 CYS A 46 -1 N TYR A 44 O PHE A 53
SHEET 3 A 5 VAL A 69 ARG A 74 -1 O LEU A 71 N ILE A 45
SHEET 4 A 5 ASP A 119 ILE A 124 -1 O LYS A 121 N HIS A 72
SHEET 5 A 5 LEU A 129 ILE A 131 -1 O ILE A 131 N ILE A 122
SHEET 1 B 5 ILE A 217 CYS A 219 0
SHEET 2 B 5 LEU A 208 ASN A 211 -1 N TRP A 209 O LEU A 218
SHEET 3 B 5 LEU A 244 LYS A 247 -1 O VAL A 246 N LEU A 210
SHEET 4 B 5 VAL A 258 SER A 260 -1 O TYR A 259 N ALA A 245
SHEET 5 B 5 ASP A 265 MET A 266 -1 O ASP A 265 N SER A 260
SHEET 1 C 2 GLN A 434 ASP A 435 0
SHEET 2 C 2 ARG C 74 GLY C 75 -1 O GLY C 75 N GLN A 434
SHEET 1 D 4 LYS A 476 ASP A 484 0
SHEET 2 D 4 PHE A 463 CYS A 471 -1 N VAL A 465 O ARG A 482
SHEET 3 D 4 ALA A 552 PHE A 562 -1 O VAL A 557 N LYS A 470
SHEET 4 D 4 GLU A 540 SER A 547 -1 N PHE A 545 O SER A 554
SHEET 1 E 5 ILE A 486 LEU A 489 0
SHEET 2 E 5 TYR A 568 ILE A 573 1 O GLN A 572 N LEU A 489
SHEET 3 E 5 ILE A 827 ARG A 832 -1 O TYR A 828 N ILE A 571
SHEET 4 E 5 LYS A 777 MET A 787 -1 N ILE A 784 O ILE A 827
SHEET 5 E 5 GLU A 596 ASP A 598 -1 N LEU A 597 O TYR A 778
SHEET 1 F 7 ILE A 486 LEU A 489 0
SHEET 2 F 7 TYR A 568 ILE A 573 1 O GLN A 572 N LEU A 489
SHEET 3 F 7 ILE A 827 ARG A 832 -1 O TYR A 828 N ILE A 571
SHEET 4 F 7 LYS A 777 MET A 787 -1 N ILE A 784 O ILE A 827
SHEET 5 F 7 HIS A 795 LYS A 802 -1 O HIS A 795 N MET A 787
SHEET 6 F 7 ARG A 805 ASN A 810 -1 O ARG A 805 N LYS A 802
SHEET 7 F 7 LYS A 813 ALA A 816 -1 O LYS A 813 N ASN A 810
SHEET 1 G 2 ALA A 525 GLN A 526 0
SHEET 2 G 2 VAL A 589 SER A 590 1 O SER A 590 N ALA A 525
SHEET 1 H 2 PHE A 576 PHE A 578 0
SHEET 2 H 2 PRO A 584 LYS A 586 -1 O LYS A 585 N THR A 577
SHEET 1 I 5 GLY B 52 GLY B 54 0
SHEET 2 I 5 LEU B 43 CYS B 46 -1 N TYR B 44 O PHE B 53
SHEET 3 I 5 VAL B 69 ARG B 74 -1 O LEU B 73 N LEU B 43
SHEET 4 I 5 ASP B 119 ILE B 124 -1 O LYS B 121 N HIS B 72
SHEET 5 I 5 LEU B 129 ALA B 132 -1 O ILE B 131 N ILE B 122
SHEET 1 J 5 ILE B 217 CYS B 219 0
SHEET 2 J 5 LEU B 208 ASN B 211 -1 N TRP B 209 O LEU B 218
SHEET 3 J 5 LEU B 244 LEU B 248 -1 O VAL B 246 N LEU B 210
SHEET 4 J 5 VAL B 258 SER B 260 -1 O TYR B 259 N ALA B 245
SHEET 5 J 5 ASP B 265 VAL B 267 -1 O ASP B 265 N SER B 260
SHEET 1 K 4 VAL B 477 ASP B 484 0
SHEET 2 K 4 PHE B 463 CYS B 471 -1 N GLU B 467 O THR B 480
SHEET 3 K 4 ALA B 552 PHE B 562 -1 O ARG B 561 N GLU B 466
SHEET 4 K 4 GLU B 540 SER B 547 -1 N VAL B 542 O ALA B 556
SHEET 1 L 5 MET B 487 LEU B 489 0
SHEET 2 L 5 TYR B 568 ILE B 573 1 O GLN B 572 N LEU B 489
SHEET 3 L 5 ILE B 827 ARG B 832 -1 O TYR B 830 N LEU B 569
SHEET 4 L 5 LYS B 777 MET B 787 -1 N ALA B 782 O PHE B 829
SHEET 5 L 5 GLU B 596 ASP B 598 -1 N LEU B 597 O TYR B 778
SHEET 1 M 7 MET B 487 LEU B 489 0
SHEET 2 M 7 TYR B 568 ILE B 573 1 O GLN B 572 N LEU B 489
SHEET 3 M 7 ILE B 827 ARG B 832 -1 O TYR B 830 N LEU B 569
SHEET 4 M 7 LYS B 777 MET B 787 -1 N ALA B 782 O PHE B 829
SHEET 5 M 7 HIS B 795 LYS B 802 -1 O HIS B 795 N MET B 787
SHEET 6 M 7 ARG B 805 ASN B 810 -1 O ARG B 805 N LYS B 802
SHEET 7 M 7 LYS B 813 ALA B 816 -1 O LYS B 813 N ASN B 810
SHEET 1 N 2 ALA B 525 GLN B 526 0
SHEET 2 N 2 VAL B 589 SER B 590 1 O SER B 590 N ALA B 525
SHEET 1 O 2 PHE B 576 PHE B 578 0
SHEET 2 O 2 PRO B 584 LYS B 586 -1 O LYS B 585 N THR B 577
SHEET 1 P 5 THR C 12 GLU C 16 0
SHEET 2 P 5 GLN C 2 LYS C 6 -1 N VAL C 5 O ILE C 13
SHEET 3 P 5 THR C 66 LEU C 69 1 O LEU C 67 N PHE C 4
SHEET 4 P 5 LEU C 43 PHE C 45 -1 N ILE C 44 O HIS C 68
SHEET 5 P 5 LYS C 48 GLN C 49 -1 O LYS C 48 N PHE C 45
SHEET 1 Q 5 THR D 12 GLU D 16 0
SHEET 2 Q 5 GLN D 2 LYS D 6 -1 N VAL D 5 O ILE D 13
SHEET 3 Q 5 THR D 66 LEU D 69 1 O LEU D 67 N LYS D 6
SHEET 4 Q 5 LEU D 43 PHE D 45 -1 N ILE D 44 O HIS D 68
SHEET 5 Q 5 LYS D 48 GLN D 49 -1 O LYS D 48 N PHE D 45
SSBOND 1 CYS A 195 CYS A 793 1555 1555 2.05
SSBOND 2 CYS B 195 CYS B 793 1555 1555 2.01
LINK SG CYS A 335 CB NEH C 76 1555 1555 1.81
LINK SG CYS B 335 CB NEH D 76 1555 1555 1.80
LINK C GLY C 75 N NEH C 76 1555 1555 1.26
LINK C GLY D 75 N NEH D 76 1555 1555 1.27
LINK SG CYS A 199 ZN ZN A 836 1555 1555 2.23
LINK SG CYS A 202 ZN ZN A 836 1555 1555 2.77
LINK SG CYS A 219 ZN ZN A 836 1555 1555 2.17
LINK ND1 HIS A 232 ZN ZN A 836 1555 1555 2.02
LINK SG CYS B 199 ZN ZN B 836 1555 1555 1.99
LINK SG CYS B 202 ZN ZN B 836 1555 1555 2.71
LINK SG CYS B 219 ZN ZN B 836 1555 1555 2.29
LINK ND1 HIS B 232 ZN ZN B 836 1555 1555 2.32
CISPEP 1 LEU A 125 PRO A 126 0 8.26
CISPEP 2 LEU B 125 PRO B 126 0 7.58
SITE 1 AC1 5 ASN A 333 CYS A 335 GLN A 433 GLY A 794
SITE 2 AC1 5 GLY C 75
SITE 1 AC2 5 ASN B 333 CYS B 335 GLN B 433 GLY B 794
SITE 2 AC2 5 GLY D 75
SITE 1 AC3 1 ARG D 74
SITE 1 AC4 4 CYS A 199 CYS A 202 CYS A 219 HIS A 232
SITE 1 AC5 4 CYS B 199 CYS B 202 CYS B 219 HIS B 232
CRYST1 68.295 188.845 207.860 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 0.014642 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005295 0.000000 0.00000
SCALE3 0.000000 0.000000 0.004811 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
